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      Exon variability of gene encoding glycerol-3-phosphate dehydrogenase ofIxodes ricinusticks

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      Parasite

      EDP Sciences

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          Abstract

          We have previously found apparent differences in Gpdh allele frequences between borrelia infected and uninfected Ixodes ricinus as revealed by native gel electrophoresis of allozyme polymorphisms. The present study deals with the genetic basis of the observed allozyme polymorphism. Multiple sequence alignment of 36 Gpdh open reading frames identified a total of 40 polymorphic nucleotide sites. Of the 40 polymorphic nucleotide sites, 34 were silent (did not result in amino acid residue change), while six were active causing a change in the amino acid chain. All polymorphic amino acid sites were situated within the N-terminal NAD-binding domain, whereas the C-terminal substrate-binding domain was highly conserved. Analysis of the obtained Gpdh sequences and GPDH allozyme polymorphisms for individual ticks pointed to amino acid changes at positions 61 (glycine-to-glutamic acid), 64 (serine-to-cysteine) and 102 (glycine-to-arginine) as a key for differential mobility of GPDH allozymes in an electric field. Our findings are discussed in the context of the molecular basis of I. ricinus host finding behavior.

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          Author and article information

          Journal
          Parasite
          Parasite
          EDP Sciences
          1252-607X
          1776-1042
          December 2010
          December 2010
          : 17
          : 4
          : 363-368
          Article
          10.1051/parasite/2010174363
          21275244
          © 2010

          This work is licensed under a Creative Commons Attribution 4.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

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          Self URI (journal page): http://www.parasite-journal.org/

          Parasitology, Life sciences

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