Title

Authors

Affiliation

Division of Biological science, School of Natural Sciences, Bangalore University, Bangalore-56005

Email

puttarajuhp@hotmail.com; *Corresponding author

Article Type

Hypothesis

Date

Received July 07, 2012; Accepted July 16, 2012; Published August 03, 2012

Wolbachia surface protein (WSP) is an eight beta-barrel transmembrane structure which participates in host immune response, cell proliferation, pathogenicity and controlled cell death program. The protein has four extracellular loops containing hyper variable regions separated by conserved regions. The WSP structure is homologous to Neisseria surface protein (Nsp A) which has about 34% similarity including antigenic variation and hydrophilicity. Recombination has a large impact on diversity of this protein including positive selection which is major constraint on protein evolution. The molecular mechanism through which Wolbachia induces various reproductive anomalies is unclear; a key feature observed for such anomalies might be because of Wolbachia undergoing extensive recombination. In Wolbachia, increased recombination is observed in ankyrin proteins, surface proteins and in some hypothetical proteins. Genetic div ergence is extensive in the WSP gene, WSP is known to be a chimeric protein involved in host-symbiont interactions. Here we predicted the structural and functional variations in WSP sequences of Wolbachia present in D. melanogaster, A. tabida and in B. malayi.

Keywords

Wolbachia, OMP, WSP, Drosophila melanogaster, Asobera tabida, Brugaria malayi, Drug target, 3D protein structure

Citation

Uday & Puttaraju, Bioinformation 8(15): 711-715 (2012)
 

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.