Open AccessEffect of Vibrio cholerae non‐O1 protease on lysozyme, lactoferrin and secretory immunoglobulin A
Author(s) -
Toma Claudia,
Honma Yasuko,
Iwanaga Masaaki
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb07979.x
Subject(s) - lactoferrin , serine protease , vibrio cholerae , protease , lysozyme , masp1 , biology , proteases , microbiology and biotechnology , biochemistry , secretory protein , cleavage (geology) , tmprss6 , chemistry , enzyme , bacteria , secretion , paleontology , genetics , fracture (geology)
The effect of Vibrio cholerae non‐O1 protease on host defense proteins (lysozyme, secretory immunoglobullin A and lactoferrin) was studied in relation to its virulence mechanism. The proteins treated with the protease were analysed by SDS‐PAGE. There was no influence of the protease on lysozyme. The protease cleaved lactoferrin into two fragments of 50 kDa and 34 kDa. N‐terminal amino acid sequencing of these fragments revealed that the cleavage site was near the hinge region, between serine 420 and serine 421. This cleavage could affect the transition from open to closed configuration which is involved in iron binding and release. The anti‐bacterial activity of lactoferrin was not affected by protease treatment. Secretory immunoglobulin A yielded a 42‐kDa protein as the cleavage product. The susceptibility of secretory immunoglobulin A to V. cholerae non‐O1 protease suggests a mechanism by which bacteria might evade the effect of this immunoglobulin.