Comparative analysis of Wolbachia surface protein in D. melanoagster, A. tabida and B. malayi

Wolbachia surface protein (WSP) is an eight beta-barrel transmembrane structure which participates in host immune response, cellproliferation, pathogenicity and controlled cell death program. The protein has four extracellular loops containing hyper variableregions separated by conserved regions. The WSP structure is homologous to Neisseria surface protein (Nsp A) which has about34% similarity including antigenic variation and hydrophilicity. Recombination has a large impact on diversity of this proteinincluding positive selection which is major constraint on protein evolution. The molecular mechanism through which Wolbachiainduces various reproductive anomalies is unclear; a key feature observed for such anomalies might be because of Wolbachiaundergoing extensive recombination. In Wolbachia, increased recombination is observed in ankyrin proteins, surface proteins and insome hypothetical proteins. Genetic divergence is extensive in the WSP gene, WSP is known to be a chimeric protein involved inhost-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.