Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 529, Issue 1, Pages 1-10Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2012.11.001
Keywords
PGRP-S; Fatty acids; Tuberculosis; Crystal structure; Binding constants
Categories
Funding
- Department of Science and Technology (DST), Ministry of Science and Technology, New Delhi
- Department of Biotechnology (DBT), Ministry of science and Technology, New Delhi
- DST
- Council of Scientific and Industrial Research
- Indian Council of Medical research, New Delhi
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Short peptidoglycan recognition protein (PGRP-S) is a member of the mammalian innate immune system. PGRP-S from Camelus dromedarius (CPGRP-S) has been shown to bind to lipopolysaccharide (LPS), lipoteichoic acid (LTA) and peptidoglycan (PGN). Its structure consists of four molecules A, B, C and D with ligand binding clefts situated at A-B and C-D contacts. It has been shown that LPS, LTA and PGN bind to CPGRP-S at C-D contact. The cleft at the A-B contact indicated features that suggested a possible binding of fatty acids including mycolic acid of Mycobacterium tuberculosis. Therefore, binding studies of CPGRP-S were carried out with fatty acids, butyric acid, lauric acid, myristic acid, stearic acid and mycolic acid which showed affinities in the range of 10(-5) to 10(-8) M. Structure determinations of the complexes of CPGRP-S with above fatty acids showed that they bound to CPGRP-S in the cleft at the A-B contact. The flow cytometric studies showed that mycolic acid induced the production of pro-inflammatory cytokines, TNF-alpha and IFN-gamma by CD3+ T cells. The concentrations of cytokines increased considerably with increasing concentrations of mycolic acid. However, their levels decreased substantially on adding CPGRP-S. (C) 2012 Elsevier Inc. All rights reserved.
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