1.C.116 The Membrane-permeabilizing Peptide, Abaecin (Abaecin) Family Honeybees (Apis mellifera) are frequently exposed to and infected by plant-associated bacteria. They produce antibacterial peptides which accumulate in the bee hemolymph. One such peptide, abacin, exhibits a broad spectrum of activities against Gram-negative plant pathogens. The highest specific activity was against an apidaecin-resistant Xanthomonas strain. In contrast to the immediate action of apidaecins, bactericidal activity is delayed (Casteels et al. 1990).
References:
Casteels, P., C. Ampe, L. Riviere, J. Van Damme, C. Elicone, M. Fleming, F. Jacobs, and P. Tempst. (1990). Isolation and characterization of abaecin, a major antibacterial response peptide in the honeybee (Apis mellifera). Eur J Biochem 187: 381-386.
Hara, S. and M. Yamakawa. (1995). A novel antibacterial peptide family isolated from the silkworm, Bombyx mori. Biochem. J. 310(Pt2): 651-656.
Examples:
TC#	Name	Organismal Type	Example
1.C.116.1.1	*Bacteriocidal peptide, Abaecin, of 53 aas (Casteels et al.* 1990).**	Insects	*Abaecin of Apis mellifera* (Honeybee)**

1.C.116.1.2	Abaecin-like protein of 117 aas	Insects	Abaecin-like protein of Pteromalus puparum

1.C.116.1.3	Nabaecin-1 of 117 aas	Insects	*Nabaecin-1 of Nasonia vitripennis* (parasitic wosp)**

1.C.116.1.4	Nabaecin-3 of 98 aas.	Insects	Nabaecin-3 of Nasonia vitripennis

Examples:
TC#	Name	Organismal Type	Example
Examples:
TC#	Name	Organismal Type	Example