@article{open2118,
          volume = {525},
          number = {1},
           month = {August},
          author = {Ranjana Tripathi and Vikas Kaithwas and Chetna Dureja and Saumya Raychaudhuri},
            note = {Copyright of this article belongs to Elsevier.},
           title = {Alanine-scanning mutagenesis of WH2 domains of VopF reveals residues important for conferring lethality in a Saccharomyces cerevisiae model.},
       publisher = {Elsevier Science Ltd},
            year = {2013},
         journal = {Gene},
           pages = {116--23},
        keywords = {ype III effector proteinVibrio cholerae},
             url = {http://crdd.osdd.net/open/2118/},
        abstract = {VopF, the type III effector molecule, has been implicated in the pathogenesis of non-O1, non-O139 strains of Vibrio cholerae. It is a protein of 530 amino acids, comprises of one formin homology 1-like (FH1-like) domain and three WASP homology 2 (WH2) domains. Previous works have demonstrated that WH2 domains are crucial for VopF function as a modulator of cellular actin homeostasis. Furthermore, domain deletion analysis also suggests that VopF variant constituted with only WH2 domain 3 is more efficient in restricting the growth of budding yeast than its congeners containing either only domain 1 or domain 2. Interestingly, a good degree of sequence diversity is present within each WH2 domain of VopF. In order to ascertain the importance of different amino acids in each WH2 domain, a systemic alanine scanning mutagenesis was employed. Using a yeast model system, the alanine derivatives of each amino acid of WH2 domain 1 and 3 of VopF were examined for growth restricting activity. Taken together, our mutagenesis results reveal the identification of critical residues of WH2 domain 1 and 3 of VopF.}
}