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The Outer Membrane Beta-barrel Endoprotease, Omptin (Omptin) Family

The Omptin family is a large family of outer membrane proteases/adhesins, found and studied primarily in enterobacteria (Kukkonen and Korhonen 2004). They play important roes in the degredation of denatured periplasmic proteins (E. coli), and funtion in pathogenesis (in Shigella, Escherichia, Yersinia and Salmonella).  In Yersinia pestis, the Pla protein is a plasminogen activator.  It both activates plasminogen and inactivating α2-antiplasmin (Suomalainen et al. 2007).  It also degrades complement components.  In E. coli, omptins, OmpT and OmpP, have been shown to cleave and inactivate cationic antimicrobial peptides (Kukkonen and Korhonen 2004).  OmpT of E. coli cleaves peptide bonds between two basic amino acids using a histidyl residue and an aspartyl residue at the active site of the protease and surprisingly, is functional in high concentrations of urea (Stathopoulos 1998; Hritonenko and Stathopoulos 2007).

The omptins Pla (Yersinia) and PgtE (Salmonella) attack innate immunity by affecting the plasminogen/plasmin, complement, coagulation, fibrinolysis, and matrix metalloproteinase systems, by inactivating antimicrobial peptides, and by enhancing bacterial adhesiveness and invasiveness (Haiko et al. 2009; Yun and Morrissey 2009; Korhonen et al. 2013). Although the mechanistic details of the functions of Pla and PgtE differ, the outcome is the same: enhanced spread and multiplication of Y. pestis and S. enterica in the host.  Maximal activity requires association with lipopolysaccharide (Hritonenko and Stathopoulos 2007).

The omptins enhance pathogenicity and attack innate immunity bynumerous mechanisms: by affecting the plasminogen/plasmin, complement, coagulation, fibrinolysis, and matrix metalloproteinase systems, by inactivating antimicrobial peptides, and by enhancing bacterial adhesiveness and invasiveness (Haiko et al. 2009; Yun and Morrissey 2009; Korhonen et al. 2013
). Although the mechanistic details of the functions of Pla and PgtE differ, the outcome is the same: enhanced spread and multiplication of Y. pestis and S. enterica in the host.  Maximal activity requires association with lipopolysaccharide (Yun and Morrissey 2009; Korhonen et al. 2013). Although the mechanistic details of the functions of Pla and PgtE differ, the outcome is the same: enhanced spread and multiplication of Y. pestis and S. enterica in the host.  Maximal activity requires association with lipopolysaccharide (Korhonen et al. 2013). Although the mechanistic details of the functions of Pla and PgtE differ, the outcome is the same: enhanced spread and multiplication of Y. pestis and S. enterica in the host.  Maximal activity requires association with lipopolysaccharide (Korhonen et al. 2013Yun and Morrissey 2009; Korhonen et al. 2013). Although the mechanistic details of the functions of Pla and PgtE differ, the outcome is the same: enhanced spread and multiplication of Y. pestis and S. enterica in the host.  Maximal activity requires association with lipopolysaccharide (Hritonenko and Stathopoulos 2007).

The omptins enhance pathogenicity and attack innate immunity bynumerous mechanisms: by affecting the plasminogen/plasmin, complement, coagulation, fibrinolysis, and matrix metalloproteinase systems, by inactivating antimicrobial peptides, and by enhancing bacterial adhesiveness and invasiveness (Haiko et al. 2009; Yun and Morrissey 2009; Korhonen et al. 2013
). Although the mechanistic details of the functions of Pla and PgtE differ, the outcome is the same: enhanced spread and multiplication of Y. pestis and S. enterica in the host.  Maximal activity requires association with lipopolysaccharide (Yun and Morrissey 2009; Korhonen et al. 2013). Although the mechanistic details of the functions of Pla and PgtE differ, the outcome is the same: enhanced spread and multiplication of Y. pestis and S. enterica in the host.  Maximal activity requires association with lipopolysaccharide (Korhonen et al. 2013). Although the mechanistic details of the functions of Pla and PgtE differ, the outcome is the same: enhanced spread and multiplication of Y. pestis and S. enterica in the host.  Maximal activity requires association with lipopolysaccharide (Korhonen et al. 2013Korhonen et al. 2013Korhonen et al. 2013). Although the mechanistic details of the functions of Pla and PgtE differ, the outcome is the same: enhanced spread and multiplication of Y. pestis and S. enterica in the host.  Maximal activity requires association with lipopolysaccharide (Hritonenko and Stathopoulos 2007).

The omptins enhance pathogenicity and attack innate immunity bynumerous mechanisms: by affecting the plasminogen/plasmin, complement, coagulation, fibrinolysis, and matrix metalloproteinase systems, by inactivating antimicrobial peptides, and by enhancing bacterial adhesiveness and invasiveness (Haiko et al. 2009; Yun and Morrissey 2009; Korhonen et al. 2013). Although the mechanistic details of the functions of Pla and PgtE differ, the outcome is the same: enhanced spread and multiplication of Y. pestis and S. enterica in the host.  Maximal activity requires association with lipopolysaccharide (Yun and Morrissey 2009; Korhonen et al. 2013). Although the mechanistic details of the functions of Pla and PgtE differ, the outcome is the same: enhanced spread and multiplication of Y. pestis and S. enterica in the host.  Maximal activity requires association with lipopolysaccharide (Korhonen et al. 2013). Although the mechanistic details of the functions of Pla and PgtE differ, the outcome is the same: enhanced spread and multiplication of Y. pestis and S. enterica in the host.  Maximal activity requires association with lipopolysaccharide (Korhonen et al. 2013Korhonen et al. 2013<Hritonenko and Stathopoulos 2007).

The omptins enhance pathogenicity and attack innate immunity bynumerous mechanisms: by affecting the plasminogen/plasmin, complement, coagulation, fibrinolysis, and matrix metalloproteinase systems, by inactivating antimicrobial peptides, and by enhancing bacterial adhesiveness and invasiveness (Haiko et al. 2009; Yun and Morrissey 2009; Korhonen et al. 2013
). Although the mechanistic details of the functions of Pla and PgtE differ, the outcome is the same: enhanced spread and multiplication of Y. pestis and S. enterica in the host.  Maximal activity requires association with lipopolysaccharide (Yun and Morrissey 2009; Korhonen et al. 2013). Although the mechanistic details of the functions of Pla and PgtE differ, the outcome is the same: enhanced spread and multiplication of Y. pestis and S. enterica in the host.  Maximal activity requires association with lipopolysaccharide (Korhonen et al. 2013). Although the mechanistic details of the functions of Pla and PgtE differ, the outcome is the same: enhanced spread and multiplication of Y. pestis and S. enterica in the host.  Maximal activity requires association with lipopolysaccharide (Korhonen et al. 2013Korhonen et al. 2013Korhonen et al. 2013). Although the mechanistic details of the functions of Pla and PgtE differ, the outcome is the same: enhanced spread and multiplication of Y. pestis and S. enterica in the host.  Maximal activity requires association with lipopolysaccharide (Yun and Morrissey 2009; Korhonen et al. 2013). Although the mechanistic details of the functions of Pla and PgtE differ, the outcome is the same: enhanced spread and multiplication of Y. pestis and S. enterica in the host.  Maximal activity requires association with lipopolysaccharide (Korhonen et al. 2013). Although the mechanistic details of the functions of Pla and PgtE differ, the outcome is the same: enhanced spread and multiplication of Y. pestis and S. enterica in the host.  Maximal activity requires association with lipopolysaccharide (Korhonen et al. 2013Korhonen et al. 2013<Korhonen et al. 2013). Although the mechanistic details of the functions of Pla and PgtE differ, the outcome is the same: enhanced spread and multiplication of Y. pestis and S. enterica in the host.  Maximal activity requires association with lipopolysaccharide (Korhonen et al. 2013Korhonen et al. 2013Korhonen et al. 2013Korhonen et al. 2013Korhonen et al. 2013).

References associated with 9.B.50 family:

Haiko, J., M. Suomalainen, T. Ojala, K. Lähteenmäki, and T.K. Korhonen. (2009). Invited review: Breaking barriers--attack on innate immune defences by omptin surface proteases of enterobacterial pathogens. Innate Immun 15: 67-80. 19318417
Hritonenko, V. and C. Stathopoulos. (2007). Omptin proteins: an expanding family of outer membrane proteases in Gram-negative Enterobacteriaceae. Mol. Membr. Biol. 24: 395-406. 17710644
Korhonen, T.K., J. Haiko, L. Laakkonen, H.M. Järvinen, and B. Westerlund-Wikström. (2013). Fibrinolytic and coagulative activities of Yersinia pestis. Front Cell Infect Microbiol 3: 35. 23898467
Kukkonen, M. and T.K. Korhonen. (2004). The omptin family of enterobacterial surface proteases/adhesins: from housekeeping in Escherichia coli to systemic spread of Yersinia pestis. Int. J. Med. Microbiol. 294: 7-14. 15293449
Stathopoulos, C. (1998). Structural features, physiological roles, and biotechnological applications of the membrane proteases of the OmpT bacterial endopeptidase family: a micro-review. Membr Cell Biol 12: 1-8. 9829254
Suomalainen, M., J. Haiko, P. Ramu, L. Lobo, M. Kukkonen, B. Westerlund-Wikström, R. Virkola, K. Lähteenmäki, and T.K. Korhonen. (2007). Using every trick in the book: the Pla surface protease of Yersinia pestis. Adv Exp Med Biol 603: 268-278. 17966423
Yun, T.H. and J.H. Morrissey. (2009). Polyphosphate and omptins: novel bacterial procoagulant agents. J Cell Mol Med 13: 4146-4153. 19725923