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STUDY OF MOLECULAR SURFACE PROPERTY OF PHOSPHOLIPASE A2 (PLA2) FROM NAJA NAJA
Authors: Gomase V.S., Gangawane A.K., More A.R.
Number of views: 359
This study was designed to elucidate the signalling pathways by which secretary phospholipase
a2 (sPLA2s) induce in vitro neutrophil migration and PLA2 inhibits platelet aggregation in PRP and explains
the decreased clot retraction and retarded and compromised elasticity build up. Naja naja venoms are
complex and contain several toxic components, including neurotoxins and phospholipases A2 that cause
post-synaptic neuromuscular blockade with respiratory paralysis and cardiac arrest. The antigenic epitopes
on phospholipase a2 (Pla2) are important determinant of protection against venom. In this analysis, we
found the antigenic epitopes 29-GRGGSGTPVDD-39, 77-TCKGDNNACA-86, of protein called the antigenic
determinant or the epitope is sufficient for eliciting the desired immune response. Also predict the MHC
binder and these MHC Class peptide segments are from a set of aligned peptides known to bind to a given
major histocompatibility complex (MHC) molecule as the predictor of MHC-peptide binding. Binding ability
prediction of antigen peptides to MHC class molecules is important in vaccine development. The method
integrates prediction of peptide MHC class binding; proteasomal C terminal cleavage efficiency of protein.