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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.