Literaturdatenbank
Literaturdatenbank |
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Chattopadhyay, S., Sinha, N. K., Banerjee, S., Roy, D., Chattopadhyay, D., & Roy, S. (2006). Small cationic protein from a marine turtle has beta-defensin-like fold and antibacterial and antiviral activity. Proteins:- Structure Function and Bioinformatics, 64(2), 524–531.
Added by: Sarina Wunderlich (23 Dec 2008 22:49:57 UTC) |
| Resource type: Journal Article DOI: 10.1002/prot.20963 BibTeX citation key: Chattopadhyay2006 View all bibliographic details  |
Categories: General Keywords: Caretta, Caretta caretta, Cheloniidae, Schildkröten = turtles + tortoises Creators: Banerjee, Chattopadhyay, Chattopadhyay, Roy, Roy, Sinha Collection: Proteins:- Structure Function and Bioinformatics |
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| Abstract |
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Egg white of marine turtle Caretta caretta contains a small cationic protein but lacks lysozyme. The protein was sequenced by a combination of sequential Edman degradation, carboxypeptidase digestion, nuclear magnetic resonance (NMR) and electrospray ionization tandem mass spectrometry. The protein contains 36 amino acid residues of which six are half-cysteines. The three-dimensional structure of the protein was deduced from two-dimensional NMR experiments and was observed to be similar to vertebrate -defensins. However, disulfide connectivity is C1-C6/C2-C5/C3-C4; different from that of the vertebrate -defensins. The protein showed strong antibacterial activity against Escherichia coli and Salmonella typhimurium. The protein also showed significant antiviral activity against an enveloped rhabdovirus, Chandipura virus, which is an emerging human pathogen. This virus is also closely related to the vesicular stomatitis virus, whose growth was also inhibited. This small cationic protein is part of the innate immunity of this organism and replaces lysozyme in the egg. It has the potential to be developed as an antibacterial and antiviral agent. Keywords: NMR • structure • Chandipura • E. coli • disulfide • cationic Added by: Sarina Wunderlich |
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Added by: Sarina Wunderlich |