TCDB is operated by the Saier Lab Bioinformatics Group

1.B.1 The General Bacterial Porin (GBP) Family

OMP porins are present in the outer membranes of Gram-negative bacteria, mitochondria and plastids. They catalyze the energy-independent facilitation of small (Mr of <1000 Da) molecules across the outer membranes of bacteria and organelles with variable degrees of selectivity. The structurally characterized members of this functional superfamily usually consist of homotrimeric proteins with subunits that are of 250-450 amino acyl residues in length. The high resolution three-dimensional structures of several of these proteins are known. These proteins include OmpC, OmpF and PhoP of E. coli. They form 16-stranded antiparallel β-barrel structures with all β-strands hydrogen-bonded to their nearest neighbors along the chain. Each trimer consists of three channels, each with the β-barrel perpendicular to the plane of the membrane. Polypeptide loops lining the inner barrel wall restrict the channel width, thereby defining the diffusion properties of the pore. Some porins are cation-selective, others are anion-selective and still others are selective for specific compounds (e.g., sugars, nucleotides, phosphate, pyrophosphate). Sequence comparisons and three-dimensional structural analyses suggest that many of the families described under category 1.B are related (see porin superfamilies in TCDB and (Reddy and Saier 2016). Outer membrane porins have been reviewed (Masi et al. 2019; Vergalli et al. 2019). Hermansen et al. 2022 have summarized the knowledge of beta-barrel structure and folding and give an overview of their functions, evolution, and potential as drug targets. Larger porins can be made from smaller porins using a loop-to-hairpin mechanism (Dhar et al. 2023). Gating of beta-barrel protein pores, porins and channels has been reviewed (Mayse and Movileanu 2023).  Structural bioinformatic studies of bacterial outer membrane beta-barrel porins have been conducted (Sajeev-Sheeja et al. 2023).

β-barrel membrane proteins perform a variety of functions, such as mediating non-specific, passive transport of ions and small molecules, selectively passing molecules like maltose and sucrose, and can form voltage dependent anion channels. Understanding the structural features of β-barrel membrane proteins and detecting them in genomic sequences are challenging tasks in structural and functional genomics. With the survey of experimentally known amino acid sequences and structures, the characteristic features of amino acid residues in β-barrel membrane proteins and novel parameters for understanding their folding and stability have been described by Gromiha and Suwa (2007). Statistical methods and machine learning techniques discriminate β-barrel membrane proteins from other folding types of globular and membrane proteins. Different methods including hydrophobicity profiles, rule based approach, amino acid properties, neural networks, hidden Markov models etc., predict membrane spanning segments of β-barrel membrane proteins. Discrimination techniques for detecting β-barrel membrane proteins in genomic sequences are discussed by Gromiha and Suwa (2007).

Vibrio furnissii possesses an outer membrane porin that is induced by β1,4-N-acetyl glucosamine (GlcNAc) oligomers of two to six sugar units, hydrolysis products of chitinase action on chitin (Keyhani et al., 2000). This porin is required for growth on (GlcNAc)3, and it transports acetylated chitobiose analogues, suggesting that it is specific for these oligosaccharides. It forms a subfamily (TC #1.B.1.7.1) of the GBP family. Another porin, OmpP2 of Haemophilus influenzae (TC # 1.B.1.3.2), shows specificity for nicotinamide-derived nucleotide substrates (Andersen et al., 2003).

Gram-negative Legionella pneumophila produces a siderophore (legiobactin) that promotes lung infection. lbtA and lbtB are required for the synthesis and secretion of legiobactin. An iron-repressed gene (lbtU) is directly upstream of the lbtAB-containing operon. LbtU is an outer membrane protein consisting of a 16-stranded transmembrane β-barrel, multiple extracellular domains, and short periplasmic tails. Although replicating normally, lbtU mutants, like lbtA mutants, were impaired for growth on iron-depleted media and would not take up Fe3+ legiobactin. It is the Legionella siderophore receptor.

The generalized transport reaction catalyzed by porins is:

Solute (out) Solute (in)

References associated with 1.B.1 family:

Andersen, C., E. Maier, G. Kemmer, J. Blass, A.-K. Hilpert, R. Benz, and J. Reidl. (2003). Porin OmpP2 of Haemophilus influenzae shows specificity for nicotinamide-derived nucleotide substrates. J. Biol. Chem. 278: 24269-24276. 12695515
Andrade, I.d.a.S., J.L. Vianez-Júnior, C.L. Goulart, F. Homblé, J.M. Ruysschaert, W.M. Almeida von Krüger, P.M. Bisch, W. de Souza, R. Mohana-Borges, and M.C. Motta. (2011). Characterization of a porin channel in the endosymbiont of the trypanosomatid protozoan Crithidia deanei. Microbiology 157: 2818-2830. 21757490
Aunkham, A., A. Schulte, M. Winterhalter, and W. Suginta. (2014). Porin involvement in cephalosporin and carbapenem resistance of Burkholderia pseudomallei. PLoS One 9: e95918. 24788109
Aunkham, A., A. Schulte, W.C. Sim, W. Chumjan, and W. Suginta. (2020). Vibrio campbellii chitoporin: Thermostability study and implications for the development of therapeutic agents against Vibrio infections. Int J Biol Macromol. [Epub: Ahead of Print] 32858106
Aunkham, A., M. Zahn, A. Kesireddy, K.R. Pothula, A. Schulte, A. Baslé, U. Kleinekathöfer, W. Suginta, and B. van den Berg. (2018). Structural basis for chitin acquisition by marine Vibrio species. Nat Commun 9: 220. 29335469
Bajaj, H., Q.T. Tran, K.R. Mahendran, C. Nasrallah, J.P. Colletier, A. Davin-Regli, J.M. Bolla, J.M. Pagès, and M. Winterhalter. (2012). Antibiotic uptake through membrane channels: role of Providencia stuartii OmpPst1 porin in carbapenem resistance. Biochemistry 51: 10244-10249. 23210483
Bartsch, A., S. Llabrés, F. Pein, C. Kattner, M. Schön, M. Diehn, M. Tanabe, A. Munk, U. Zachariae, and C. Steinem. (2019). High-resolution experimental and computational electrophysiology reveals weak β-lactam binding events in the porin PorB. Sci Rep 9: 1264. 30718567
Benz, R., R.P. Darveau, and R.E.W. Hancock. (1984). Outer-membrane protein PhoE from Escherichia coli forms anion-selective pores in lipid-bilayer membranes. Eur. J. Biochem. 140: 319-324. 6325185
Blasband, A.J. and C.A. Schnaitman. (1987). Regulation in Escherichia coli of the porin protein gene encoded by lambdoid bacteriophages. J. Bacteriol. 169: 2171-2176. 3032909
Bornet, C., N. Saint, L. Fetnaci, M. Dupont, A. Davin-Régli, C. Bollet, and J.M. Pagès. (2004). Omp35, a new Enterobacter aerogenes porin involved in selective susceptibility to cephalosporins. Antimicrob. Agents Chemother. 48: 2153-2158. 15155215
Brunen, M., H. Engelhardt, A. Schmid, and R. Benz. (1991). The major outer membrane protein of Acidovorax delafieldii is an anion-selective porin. J. Bacteriol. 173: 4182-4187. 1712013
Brunson, D.N., E. Maldosevic, A. Velez, E. Figgins, and T.N. Ellis. (2019). Porin loss in Klebsiella pneumoniae clinical isolates impacts production of virulence factors and survival within macrophages. Int. J. Med. Microbiol. 309: 213-224. 31010630
Calderón, I.L., E. Morales, N.J. Caro, C.A. Chahúan, B. Collao, F. Gil, J.M. Villarreal, F. Ipinza, G.C. Mora, and C.P. Saavedra. (2010). Response regulator ArcA of Salmonella enterica serovar Typhimurium downregulates expression of OmpD, a porin facilitating uptake of hydrogen peroxide. Res. Microbiol. 162: 214-222. 21144897
Cervera, J., A.G. Komarov, and V.M. Aguilella. (2008). Rectification properties and pH-dependent selectivity of meningococcal class 1 porin. Biophys. J. 94: 1194-1202. 17965131
Chang HK., Dennis JJ. and Zylstra GJ. (2009). Involvement of two transport systems and a specific porin in the uptake of phthalate by Burkholderia spp. J Bacteriol. 191(14):4671-3. 19429613
Chatfield, C.H., B.J. Mulhern, D.M. Burnside, and N.P. Cianciotto. (2011). Legionella pneumophila LbtU acts as a novel, TonB-independent receptor for the legiobactin siderophore. J. Bacteriol. 193: 1563-1575. 21278293
Chistyulin, D.K., O.D. Novikova, E.A. Zelepuga, V.A. Khomenko, G.N. Likhatskaya, O.Y. Portnyagina, and Y.N. Antonenko. (2019). An Abnormally High Closing Potential of the OMPF Porin Channel from Yersinia Ruckeri: The Role of Charged Residues and Intramolecular Bonds. Acta Naturae 11: 89-98. 31720021
Chumjan W., Winterhalter M., Schulte A., Benz R. and Suginta W. (2015). Chitoporin from the Marine Bacterium Vibrio harveyi: PROBING THE ESSENTIAL ROLES OF TRP136 AT THE SURFACE OF THE CONSTRICTION ZONE. J Biol Chem. 290(31):19184-96. 26082491
Chumjan, W., M. Winterhalter, and W. Suginta. (2019). Effects of H-bonds on sugar binding to chitoporin from Vibrio harveyi. Biochim. Biophys. Acta. Biomembr 1861: 610-618. 30576623
Cowan, S.W., T. Schirmer, G. Rummel, M. Steiert, R. Ghosh, R.A. Pauptit, J.N. Jansonius, and J.P. Rosenbusch. (1992). Crystal structures explain functional properties of two E. coli porins. Nature 358: 727-733. 1380671
Dam, S., J.M. Pagès, and M. Masi. (2017). Dual Regulation of the Small RNA MicC and the Quiescent Porin OmpN in Response to Antibiotic Stress in Escherichia coli. Antibiotics (Basel) 6:. 29211019
Dé, E., A. Baslé, M. Jaquinod, N. Saint, M. Malléa, G. Molle, and J.M. Pagès. (2001). A new mechanism of antibiotic resistance in Enterobacteriaceae induced by a structural modification of the major porin. Mol. Microbiol. 41: 189-198. 11454211
Delcour, A.H. (1997). Function and modulation of bacterial porins: insights from electrophysiology. FEMS Microbiol. Lett. 152: 115-123. 9228742
Dhar, V., S. Gandhi, S.C. Sakharwade, A. Chawla, and A. Mukhopadhaya. (2023). Vibrio cholerae Porin OmpU Activates Dendritic Cells via TLR2 and the NLRP3 Inflammasome. Infect. Immun. 91: e0033222. 36794951
Donoghue, A., M. Winterhalter, and T. Gutsmann. (2023). Influence of Membrane Asymmetry on OmpF Insertion, Orientation and Function. Membranes (Basel) 13:. 37233578
Duperthuy, M., A.E. Sjöström, D. Sabharwal, F. Damghani, B.E. Uhlin, and S.N. Wai. (2013). Role of the Vibrio cholerae matrix protein Bap1 in cross-resistance to antimicrobial peptides. PLoS Pathog 9: e1003620. 24098113
Duret, G. and A.H. Delcour. (2010). Size and dynamics of the Vibrio cholerae porins OmpU and OmpT probed by polymer exclusion. Biophys. J. 98: 1820-1829. 20441745
Easton, D.M., A. Smith, S.G. Gallego, A.R. Foxwell, A.W. Cripps, and J.M. Kyd. (2005). Characterization of a novel porin protein from Moraxella catarrhalis and identification of an immunodominant surface loop. J. Bacteriol. 187: 6528-6535. 16159786
Egger, L.A., H. Park, and M. Inouye. (1997). Signal transduction via the histidyl-aspartyl phosphorelay. Genes Cells 2: 167-184. 9189755
El-Khatib, M., C. Nasrallah, J. Lopes, Q.T. Tran, G. Tetreau, H. Basbous, D. Fenel, B. Gallet, M. Lethier, J.M. Bolla, J.M. Pagès, M. Vivaudou, M. Weik, M. Winterhalter, and J.P. Colletier. (2018). Porin self-association enables cell-to-cell contact in floating communities. Proc. Natl. Acad. Sci. USA 115: E2220-E2228. 29476011
Elazar, M., D. Halfon, I. Pechatnikov, and Y. Nitzan. (2007). Porin isolated from the outer membrane of Erwinia amylovora and its encoding gene. Curr. Microbiol. 54: 155-161. 17211539
Fàbrega, A., J.L. Rosner, R.G. Martin, M. Solé, and J. Vila. (2012). SoxS-dependent coregulation of ompN and ydbK in a multidrug-resistant Escherichia coli strain. FEMS Microbiol. Lett. 332: 61-67. 22515487
Fernández-Mora, M., J.L. Puente, and E. Calva. (2004). OmpR and LeuO positively regulate the Salmonella enterica serovar Typhi ompS2 porin gene. J. Bacteriol. 186: 2909-2920. 15126450
Forst, S., J. Waukau, G. Leisman, M. Exner, and R. Hancock. (1995). Functional and regulatory analysis of the OmpF-like porin, OpnP, of the symbiotic bacterium Xenorhabdus nematophilus. Mol. Microbiol. 18: 779-789. 8817498
Forst, S.A. and N. Tabatabai. (1997). Role of the histidine kinase, EnvZ, in the production of outer membrane proteins in the symbiotic-pathogenic bacterium Xenorhabdus nematophilus. Appl. Environ. Microbiol. 63: 962-968. 9055414
Fralick, J.A., D.L. Diedrich, and S. Casey-Wood. (1990). Isolation of an Lc-specific Escherichia coli bacteriophage. J. Bacteriol. 172: 1660-1662. 1689719
Ganguly B., Tewari K. and Singh R. (2015). Homology modeling, functional annotation and comparative genomics of outer membrane protein H of Pasteurella multocida. J Theor Biol. 386:18-24. 26362105
Gao, T., L. Ju, J. Yin, and H. Gao. (2015). Positive regulation of the Shewanella oneidensis OmpS38, a major porin facilitating anaerobic respiration, by Crp and Fur. Sci Rep 5: 14263. 26381456
García-Sureda, L., A. Doménech-Sánchez, M. Barbier, C. Juan, J. Gascó, and S. Albertí. (2011). OmpK26, a novel porin associated with carbapenem resistance in Klebsiella pneumoniae. Antimicrob. Agents Chemother. 55: 4742-4747. 21807980
Gensberg, K., A.W. Smith, F.S. Brinkman, and R.E. Hancock. (1999). Identification of oprG, a gene encoding a major outer membrane protein of Pseudomonas aeruginosa. J. Antimicrob. Chemother. 43: 607-608. 10350397
Ghale G., Lanctot AG., Kreissl HT., Jacob MH., Weingart H., Winterhalter M. and Nau WM. (2014). Chemosensing ensembles for monitoring biomembrane transport in real time. Angew Chem Int Ed Engl. 53(10):2762-5. 24469927
Golla, V.K., E. Sans-Serramitjana, K.R. Pothula, L. Benier, J.A. Bafna, M. Winterhalter, and U. Kleinekathöfer. (2019). Fosfomycin Permeation through the Outer Membrane Porin OmpF. Biophys. J. 116: 258-269. 30616836
Goulart, C.L., P.M. Bisch, W.M. von Krüger, and F. Homblé. (2015). VCA1008: An Anion-Selective Porin of Vibrio Cholerae. Biochim. Biophys. Acta. 1848: 680-687. 25462170
Gromiha, M.M., and M. Suwa (2007). Current developments on β- barrel membrane proteins: sequence and structure analysis, discrimination and prediction. Curr. Protein Pept. Sci. 8: 580-599. 18220845
Gulati, A., R. Kumar, and A. Mukhopadhaya. (2019). Differential Recognition of OmpU by Toll-Like Receptors in Monocytes and Macrophages for the Induction of Proinflammatory Responses. Infect. Immun. 87:. 30804101
Gupta S., Prasad GV. and Mukhopadhaya A. (2015). Vibrio cholerae Porin OmpU Induces Caspase-independent Programmed Cell Death upon Translocation to the Host Cell Mitochondria. J Biol Chem. 290(52):31051-68. 26559970
Hadi-Alijanvand, H. and M. Rouhani. (2015). Journey of Poly-Nucleotides through OmpF Porin. J Phys Chem B 119: 6113-6128. 25965338
Hamzaoui, Z., A. Ocampo-Sosa, M.F. Martinez, S. Landolsi, S. Ferjani, E. Maamar, M. Saidani, A. Slim, L. Martinez-Martinez, and I.B. Boubaker. (2018). Role of association of OmpK35 and OmpK36 alteration and bla and/or bla in conferring carbapenem resistance among non-producing carbapenemase-Klebsiella pneumoniae. Int J Antimicrob Agents. [Epub: Ahead of Print] 29621592
Hermansen, S., D. Linke, and J.C. Leo. (2022). Transmembrane β-barrel proteins of bacteria: From structure to function. Adv Protein Chem Struct Biol 128: 113-161. 35034717
Housden, N.G., J.A. Wojdyla, J. Korczynska, I. Grishkovskaya, N. Kirkpatrick, A.M. Brzozowski, and C. Kleanthous. (2010). Directed epitope delivery across the Escherichia coli outer membrane through the porin OmpF. Proc. Natl. Acad. Sci. USA 107: 21412-21417. 21098297
Housden, N.G., J.T. Hopper, N. Lukoyanova, D. Rodriguez-Larrea, J.A. Wojdyla, A. Klein, R. Kaminska, H. Bayley, H.R. Saibil, C.V. Robinson, and C. Kleanthous. (2013). Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF. Science 340: 1570-1574. 23812713
Housden, N.G., P. Rassam, S. Lee, F. Samsudin, R. Kaminska, C. Sharp, J.D. Goult, M.L. Francis, S. Khalid, H. Bayley, and C. Kleanthous. (2018). Directional Porin Binding of Intrinsically Disordered Protein Sequences Promotes Colicin Epitope Display in the Bacterial Periplasm. Biochemistry 57: 4374-4381. 29949342
Hu, W.S., H.W. Chen, R.Y. Zhang, C.Y. Huang, and C.F. Shen. (2011). The expression levels of outer membrane proteins STM1530 and OmpD, which are influenced by the CpxAR and BaeSR two-component systems, play important roles in the ceftriaxone resistance of Salmonella enterica serovar Typhimurium. Antimicrob. Agents Chemother. 55: 3829-3837. 21646491
Jadhav, S.R., K.S. Rao, Y. Zheng, R.M. Garavito, and R.M. Worden. (2013). Voltage dependent closure of PorB class II porin from Neisseria meningitidis investigated using impedance spectroscopy in a tethered bilayer lipid membrane interface. J Colloid Interface Sci 390: 211-216. 23083768
Jasim, R., M.A. Baker, Y. Zhu, M. Han, E.K. Schneider-Futschik, M. Hussein, D. Hoyer, J. Li, and T. Velkov. (2018). A Comparative Study of Outer Membrane Proteome between Paired Colistin-Susceptible and Extremely Colistin-Resistant Klebsiella pneumoniae Strains. ACS Infect Dis. [Epub: Ahead of Print] 30232886
Jeanteur, D., J.H. Lakey, and F. Pattus. (1991). The bacterial porin superfamily: sequence alignment and structure prediction. Mol. Microbiol. 5: 2153-2164. 1662760
Jeanteur, D., J.H. Lakey, and F. Pattus. (1994). The porin superfamily: diversity and common features. In: Bacterial Cell Wall (J.M.Ghuysen and R. Hakenbeck, eds.). Elsevier, Amsterdam, pp. 363-380.
Kattner C., Zaucha J., Jaenecke F., Zachariae U. and Tanabe M. (2013). Identification of a cation transport pathway in Neisseria meningitidis PorB. Proteins. 81(5):830-40. 23255122
Kattner, C., S. Pfennig, P. Massari, and M. Tanabe. (2015). One-step purification and porin transport activity of the major outer membrane proteins P2 from Haemophilus influenzae, FomA from Fusobacterium nucleatum and PorB from Neisseria meningitidis. Appl Biochem Biotechnol 175: 2907-2915. 25575589
Kesireddy, A., K.R. Pothula, J. Lee, D.S. Patel, M. Pathania, B. van den Berg, W. Im, and U. Kleinekathöfer. (2019). Modeling of Specific Lipopolysaccharide Binding Sites on a Gram-Negative Porin. J Phys Chem B 123: 5700-5708. 31260306
Keyhani, N.O., X.B. Li, and S. Roseman. (2000). Chitin catabolism in the marine bacterium Vibrio furnissii. Identification and molecular cloning of a chitoporin. J. Biol. Chem. 275: 33068-33076. 10913115
Koebnik, R., K.P. Locher, and P. Van Gelder. (2000). Structure and function of bacterial outer membrane proteins: barrels in a nutshell. Mol. Microbiol. 37: 239-253. 10931321
Lee, S., N.G. Housden, S.A. Ionescu, M.H. Zimmer, R. Kaminska, C. Kleanthous, and H. Bayley. (2020). Transmembrane Epitope Delivery by Passive Protein Threading through the Pores of the OmpF Porin Trimer. J. Am. Chem. Soc. 142: 12157-12166. 32614588
Liko, I., M.T. Degiacomi, S. Lee, T.D. Newport, J. Gault, E. Reading, J.T.S. Hopper, N.G. Housden, P. White, M. Colledge, A. Sula, B.A. Wallace, C. Kleanthous, P.J. Stansfeld, H. Bayley, J.L.P. Benesch, T.M. Allison, and C.V. Robinson. (2018). Lipid binding attenuates channel closure of the outer membrane protein OmpF. Proc. Natl. Acad. Sci. USA 115: 6691-6696. 29891712
Lou, H., M. Chen, S.S. Black, S.R. Bushell, M. Ceccarelli, T. Mach, K. Beis, A.S. Low, V.A. Bamford, I.R. Booth, H. Bayley, and J.H. Naismith. (2011). Altered antibiotic transport in OmpC mutants isolated from a series of clinical strains of multi-drug resistant E. coli. PLoS One 6: e25825. 22053181
Lovelle, M., T. Mach, K.R. Mahendran, H. Weingart, M. Winterhalter, and P. Gameiro. (2011). Interaction of cephalosporins with outer membrane channels of Escherichia coli. Revealing binding by fluorescence quenching and ion conductance fluctuations. Phys Chem Chem Phys 13: 1521-1530. 21152583
Lv, T., F. Dai, Q. Zhuang, X. Zhao, Y. Shao, M. Guo, Z. Lv, C. Li, and W. Zhang. (2020). Outer membrane protein OmpU is related to iron balance in Vibrio alginolyticus. Microbiol Res 230: 126350. 31629270
Manoharan-Basil, S.S., Z. Gestels, S. Abdellati, E.A. Akomoneh, and C. Kenyon. (2023). Evidence of horizontal gene transfer within in 19 018 whole-genome spp. isolates: a global phylogenetic analysis. Microb Genom 9:. 37294009
Masi, M., M. Winterhalter, and J.M. Pagès. (2019). Outer Membrane Porins. Subcell Biochem 92: 79-123. 31214985
Massari, P., C.A. King, A.Y. Ho, and L.M. Wetzler. (2003). Neisserial PorB is translocated to the mitochondria of HeLa cells infected with Neisseria meningitidis and protects cells from apoptosis. Cell. Microbiol. 5: 99-109. 12580946
Mayse, L.A. and L. Movileanu. (2023). Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets. Int J Mol Sci 24:. 37569469
Milenkovic, S., J. Wang, S. Acosta-Gutierrez, M. Winterhalter, M. Ceccarelli, and I.V. Bodrenko. (2023). How the physical properties of bacterial porins match environmental conditions. Phys Chem Chem Phys 25: 12712-12722. 37098836
Nikaido, H. (1992). Porins and specific channels of bacterial outer membranes. Mol. Microbiol. 6: 435-442. 1373213
Novović, K., S. Mihajlović, M. Dinić, M. Malešević, M. Miljković, M. Kojić, and B. Jovčić. (2018). Acinetobacter spp. porin Omp33-36: Classification and transcriptional response to carbapenems and host cells. PLoS One 13: e0201608. 30071077
Pagel, M., V. Simonet, J. Li, M. Lallemand, B. Lauman, and A.H. Delcour. (2007). Phenotypic Characterization of Pore Mutants of the Vibrio cholerae Porin OmpU. J. Bacteriol. 189(23): 8593-8600. 17905973
Pal, A., L. Dhara, and A. Tripathi. (2019). Contribution of upregulation & OmpC/Ompk36 loss over the presence of towards carbapenem resistance development among pathogenic spp. Indian J Med Res 149: 528-538. 31411177
Park, H.J., S.W. Lee, and S.W. Han. (2014). Proteomic and functional analyses of a novel porin-like protein in Xanthomonas oryzae pv. oryzae. J Microbiol 52: 1030-1035. 25467121
Patel, D.S., S. Re, E.L. Wu, Y. Qi, P.E. Klebba, G. Widmalm, M.S. Yeom, Y. Sugita, and W. Im. (2016). Dynamics and Interactions of OmpF and LPS: Influence on Pore Accessibility and Ion Permeability. Biophys. J. 110: 930-938. 26910429
Pathania, M., S. Acosta-Gutierrez, S.P. Bhamidimarri, A. Baslé, M. Winterhalter, M. Ceccarelli, and B. van den Berg. (2018). Unusual Constriction Zones in the Major Porins OmpU and OmpT from Vibrio cholerae. Structure 26: 708-721.e4. 29657131
Pavez, M., C. Vieira, M.R. de Araujo, A. Cerda, L.M. de Almeida, N. Lincopan, and E.M. Mamizuka. (2016). Molecular mechanisms of membrane impermeability in clinical isolates of Enterobacteriaceae exposed to imipenem selective pressure. Int J Antimicrob Agents. [Epub: Ahead of Print] 27256585
Perini, D.A., A. Alcaraz, and M. Queralt-Martín. (2019). Lipid Headgroup Charge and Acyl Chain Composition Modulate Closure of Bacterial β-Barrel Channels. Int J Mol Sci 20:. 30764475
Prajapati, J.D., C.J.F. Solano, M. Winterhalter, and U. Kleinekathöfer. (2018). Enrofloxacin Permeation Pathways across the Porin OmpC. J Phys Chem B 122: 1417-1426. 29307192
Prilipov, A., P.S. Phale, R. Koebnik, C. Widmer, and J.P. Rosenbusch. (1998). Identification and characterization of two quiescent porin genes, nmpC and ompN, in Escherichia coli BE. J. Bacteriol. 180: 3388-3392. 9642192
Rassam, P., K.R. Long, R. Kaminska, D.J. Williams, G. Papadakos, C.G. Baumann, and C. Kleanthous. (2018). Intermembrane crosstalk drives inner-membrane protein organization in Escherichia coli. Nat Commun 9: 1082. 29540681
Reddy, B.L. and M.H. Saier, Jr. (2016). Properties and Phylogeny of 76 Families of Bacterial and Eukaryotic Organellar Outer Membrane Pore-Forming Proteins. PLoS One 11: e0152733. 27064789
Rodríguez-Morales, O., M. Fernández-Mora, I. Hernández-Lucas, A. Vázquez, J.L. Puente, and E. Calva. (2006). Salmonella enterica serovar Typhimurium ompS1 and ompS2 mutants are attenuated for virulence in mice. Infect. Immun. 74: 1398-1402. 16428792
Rumbo, C., M. Tomás, E. Fernández Moreira, N.C. Soares, M. Carvajal, E. Santillana, A. Beceiro, A. Romero, and G. Bou. (2014). The Acinetobacter baumannii Omp33-36 porin is a virulence factor that induces apoptosis and modulates autophagy in human cells. Infect. Immun. 82: 4666-4680. 25156738
Sajeev-Sheeja, A., E. Smorodina, and S. Zhang. (2023). Structural bioinformatics studies of bacterial outer membrane β-barrel transporters and their AlphaFold2 predicted water-soluble QTY variants. PLoS One 18: e0290360. 37607179
Santiviago, C.A., J.A. Fuentes, S.M. Bueno, A.N. Trombert, A.A. Hildago, L.T. Socias, P. Youderian, and G.C. Mora. (2002). The Salmonella enterica sv. Typhimurium smvA, yddG and ompD (porin) genes are required for the efficient efflux of methyl viologen. Mol. Microbiol. 46: 687-698. 12410826
Schulz, G.E. (1996). Porins: general to specific, native to engineered passive pores. Curr. Opin. Struc. Biol. 6: 485-490. 8794162
Simonet, V.C., A. Baslé, K.E. Klose, and A.H. Delcour. (2003). The Vibrio cholerae porins OmpU and OmpT have distinct channel properties. J. Biol. Chem. 278: 17539-17545. 12606562
Smani, Y., J. Dominguez-Herrera, and J. Pachón. (2013). Association of the outer membrane protein Omp33 with fitness and virulence of Acinetobacter baumannii. J Infect Dis 208: 1561-1570. 23908480
Solov''eva, T.F., N.M. Tischenko, V.A. Khomenko, O.Y. Portnyagina, N.Y. Kim, G.N. Likhatskaya, O.D. Novikova, and M.P. Isaeva. (2014). Study of effect of substitution of the penultimate amino acid residue on expression, structure, and functional properties of Yersinia pseudotuberculosis OmpY porin. Biochemistry (Mosc) 79: 694-705. 25108332
Solov'eva, T., G. Likhatskaya, V. Khomenko, K. Guzev, N. Kim, E. Bystritskaya, O. Novikova, A. Stenkova, A. Rakin, and M. Isaeva. (2017). The impact of length variations in the L2 loop on the structure and thermal stability of non-specific porins: The case of OmpCs from the Yersinia pseudotuberculosis complex. Biochim. Biophys. Acta. 1860: 515-525. [Epub: Ahead of Print] 29038023
Solov'eva, T.F., G.N. Likhatskaya, V.A. Khomenko, A.M. Stenkova, N.Y. Kim, O.Y. Portnyagina, O.D. Novikova, E.V. Trifonov, E.A. Nurminski, and M.P. Isaeva. (2011). A novel OmpY porin from Yersinia pseudotuberculosis: structure, channel-forming activity and trimer thermal stability. J Biomol Struct Dyn 28: 517-533. 21142221
Song, J., C.A. Minetti, M.S. Blake, and M. Colombini. (1998). Successful recovery of the normal electrophysiological properties of PorB (class 3) porin from Neisseria meningitidis after expression in Escherichia coli and renaturation. Biochim. Biophys. Acta. 1370: 289-298. 9545584
Song, W., H. Bajaj, C. Nasrallah, H. Jiang, M. Winterhalter, J.P. Colletier, and Y. Xu. (2015). Understanding Voltage Gating of Providencia stuartii Porins at Atomic Level. PLoS Comput Biol 11: e1004255. 25955156
Srinivasan, V.B., M. Venkataramaiah, A. Mondal, V. Vaidyanathan, T. Govil, and G. Rajamohan. (2012). Functional characterization of a novel outer membrane porin KpnO, regulated by PhoBR two-component system in Klebsiella pneumoniae NTUH-K2044. PLoS One 7: e41505. 22848515
Stein, C., O. Makarewicz, J.A. Bohnert, Y. Pfeifer, M. Kesselmeier, S. Hagel, and M.W. Pletz. (2015). Three Dimensional Checkerboard Synergy Analysis of Colistin, Meropenem, Tigecycline against Multidrug-Resistant Clinical Klebsiella pneumonia Isolates. PLoS One 10: e0126479. 26067824
Suginta, W., K.R. Mahendran, W. Chumjan, E. Hajjar, A. Schulte, M. Winterhalter, and H. Weingart. (2011). Molecular analysis of antimicrobial agent translocation through the membrane porin BpsOmp38 from an ultraresistant Burkholderia pseudomallei strain. Biochim. Biophys. Acta. 1808: 1552-1559. 21078354
Suginta, W., S. Sanram, A. Aunkham, M. Winterhalter, and A. Schulte. (2021). The C2 entity of chitosugars is crucial in molecular selectivity of the Vibrio campbellii chitoporin. J. Biol. Chem. 101350. [Epub: Ahead of Print] 34715124
Tanabe, M., C.M. Nimigean, and T.M. Iverson. (2010). Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB. Proc. Natl. Acad. Sci. USA 107: 6811-6816. 20351243
Tang, X., H. Wang, F. Liu, X. Sheng, J. Xing, and W. Zhan. (2019). Recombinant outer membrane protein T (OmpT) of Vibrio ichthyoenteri, a potential vaccine candidate for flounder (Paralichthys olivaceus). Microb. Pathog. 126: 185-192. 30408491
Tran, Q.T., K.R. Mahendran, E. Hajjar, M. Ceccarelli, A. Davin-Regli, M. Winterhalter, H. Weingart, and J.M. Pagès. (2010). Implication of porins in β-lactam resistance of Providencia stuartii. J. Biol. Chem. 285: 32273-32281. 20667831
Tsugawa, H., A. Ogawa, S. Takehara, M. Kimura, and Y. Okawa. (2008). Primary structure and function of a cytotoxic outer-membrane protein (ComP) of Plesiomonas shigelloides . FEMS Microbiol. Lett. 281: 10-16. 18318838
Utsunomia, C., C. Hori, K. Matsumoto, and S. Taguchi. (2017). Investigation of the Escherichia coli membrane transporters involved in the secretion of d-lactate-based oligomers by loss-of-function screening. J Biosci Bioeng 124: 635-640. 28818426
Vergalli, J., I.V. Bodrenko, M. Masi, L. Moynié, S. Acosta-Gutiérrez, J.H. Naismith, A. Davin-Regli, M. Ceccarelli, B. van den Berg, M. Winterhalter, and J.M. Pagès. (2019). Porins and small-molecule translocation across the outer membrane of Gram-negative bacteria. Nat. Rev. Microbiol. [Epub: Ahead of Print] 31792365
Vostrikova, O.P., M.P. Isaeva, G.N. Likhatskaya, O.D. Novikova, N.Y. Kim, V.A. Khomenko, and T.F. Solov'eva. (2013). OmpC-like porin from outer membrane of Yersinia enterocolitica: molecular structure and functional activity. Biochemistry (Mosc) 78: 496-504. 23848152
Wang, J., N. Fertig, and Y.L. Ying. (2019). Real-time monitoring β-lactam/β-lactamase inhibitor (BL/BLI) mixture towards the bacteria porin pathway at single molecule level. Anal Bioanal Chem 411: 4831-4837. 30824965
Wang, S.Y., J. Lauritz, J. Jass, and D.L. Milton. (2003). Role for the major outer-membrane protein from Vibrio anguillarum in bile resistance and biofilm formation. Microbiology 149: 1061-1071. 12686648
Ward, M.J., P.R. Lambden, and J.E. Heckels. (1992). Sequence analysis and relationships between meningococcal class 3 serotype proteins and porins from pathogenic and non-pathogenic Neisserial species. FEMS Microbiol. Lett. 73: 283-289. 1330818
Wassef M., Abdelhaleim M., AbdulRahman E. and Ghaith D. (2015). The Role of OmpK35, OmpK36 Porins, and Production of beta-Lactamases on Imipenem Susceptibility in Klebsiella pneumoniae Clinical Isolates, Cairo, Egypt. Microb Drug Resist. 21(6):577-80. 25945596
Whiting, G., C. Vipond, A. Facchetti, H. Chan, and J.X. Wheeler. (2019). Measurement of surface protein antigens, PorA and PorB, in Bexsero vaccine using quantitative mass spectrometry. Vaccine. [Epub: Ahead of Print] 31839469
Wise, M.G., E. Horvath, K. Young, D.F. Sahm, and K.M. Kazmierczak. (2018). Global survey of Klebsiella pneumoniae major porins from ertapenem non-susceptible isolates lacking carbapenemases. J. Med. Microbiol. 67: 289-295. 29458684
Yadav, S.K., J.K. Meena, M. Sharma, and A. Dixit. (2016). Recombinant outer membrane protein C of Aeromonas hydrophila elicits mixed immune response and generates agglutinating antibodies. Immunol Res 64: 1087-1099. 27328672
Yamamoto-Tamura, K., I. Kawagishi, N. Ogawa, and T. Fujii. (2015). A putative porin gene of Burkholderia sp. NK8 involved in chemotaxis toward β-ketoadipate. Biosci. Biotechnol. Biochem. 79: 926-936. 25649919
Ye, Y., L. Xu, Y. Han, Z. Chen, C. Liu, and L. Ming. (2018). Mechanism for carbapenem resistance of clinical Enterobacteriaceae isolates. Exp Ther Med 15: 1143-1149. 29399114
Zachariae, U., T. Klühspies, S. De, H. Engelhardt, and K. Zeth. (2006). High resolution crystal structures and molecular dynamics studies reveal substrate binding in the porin Omp32. J. Biol. Chem. 281: 7413-7420. 16434398
Zwama, M., A. Yamaguchi, and K. Nishino. (2019). Phylogenetic and functional characterisation of the multidrug efflux pump AcrB. Commun Biol 2: 340. 31531401