IgA1 (immunoglobulin A1) antibodies are the first line of defence against microbial pathogens such as Neisseria meningitidis and Haemophilus influenzae. However, these bacteria secrete a site-specific protease that is capable of cleaving human IgA1 and interacting with other host components. The IgA proteases are released by the type V secretion pathway, which involves translocation through two membranes and an autolytic, post-translational processing step. Results reported recently throw light on the type V secretion pathway and on the roles of the multifunctional IgA protease. The IgA1 protease-recognition sequence is present within the IgA1 hinge region as well as in the variable sequence connecting the IgA1 protease to its translocator domain. Recent results suggest that neisserial IgA1 proteases are capable of cleaving substrates lacking the classical recognition sequence. This review will cover recent advances in the IgA protease field.
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Conference Article| October 26 2004
Immunoglobulin A1 proteases: a structure–function update
J.R. Sayers 1
1School of Medical and Biomedical Sciences, University of Sheffield, Henry Wellcome Laboratories for Medical Research, Beech Hill Rd, Sheffield S10 2RF, U.K.
1To whom correspondence should be addressed (email J.R.Sayers@sheffield.ac.uk).
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Publisher: Portland Press Ltd
Received: July 27 2004
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2004 The Biochemical Society
H.K. Parsons, S. Vitovski, J.R. Sayers; Immunoglobulin A1 proteases: a structure–function update. Biochem Soc Trans 1 November 2004; 32 (6): 1130–1132. doi: https://doi.org/10.1042/BST0321130
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