Identification and Molecular Characterization of Molluskin, a Histone-H2A-Derived Antimicrobial Peptide from Molluscs
Author(s) -
Naveen Sathyan,
Rosamma Philip,
E. R. Chaithanya,
P. R. Anil Kumar
Publication year - 2012
Publication title -
isrn molecular biology
Language(s) - English
Resource type - Journals
ISSN - 2090-7907
DOI - 10.5402/2012/219656
Subject(s) - antimicrobial peptides , biology , innate immune system , oyster , antimicrobial , peptide sequence , histone , peptide , amino acid , complementary dna , biochemistry , microbiology and biotechnology , gene , ecology , receptor
Antimicrobial peptides are humoral innate immune components of molluscs that provide protection against pathogenic microorganisms. Among these, histone-H2A-derived antimicrobial peptides are known to actively participate in host defense responses of molluscs. Present study deals with identification of putative antimicrobial sequences from the histone-H2A of back-water oyster Crassostrea madrasensis , rock oyster Saccostrea cucullata , grey clam Meretrix casta , fig shell Ficus gracilis , and ribbon bullia Bullia vittata . A 75 bp fragment encoding 25 amino acid residues was amplified from cDNA of these five bivalves and was named “Molluskin.” The 25 amino acid peptide exhibited high similarity to previously reported histone-H2A-derived AMPs from invertebrates indicating the presence of an antimicrobial sequence motif. Physicochemical properties of the peptides are in agreement with the characteristic features of antimicrobial peptides, indicating their potential role in innate immunity of molluscs.
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