Exon variability of gene encoding glycerol-3-phosphate dehydrogenase of ixodes ricinus ticks
Apstrakt
We have previously found apparent differences in Gpdh allele frequences between borrelia infected and uninfected Ixodes riotous 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 a...n electric field. Our findings are discussed in the context of the molecular basis of I. ricinus host finding behavior.
Ključne reči:
glycerol-3-phosphate dehydrogenase / variability / Ixodes ricinusIzvor:
Parasite, 2010, 17, 4, 363-368Izdavač:
- EDP Sciences S A, Les Ulis Cedex A
Finansiranje / projekti:
- Infekcije intercelularnim mikroorganizmima rastućeg značaja: transmisija, odnos patogen-domaćin, molekularna epidemiologija i klinički značaj (RS-MESTD-MPN2006-2010-145002)
- European Commission, EU 6th Framework Programme [FP6-INCO-CT-2006-043702-SERBPARZOON]
DOI: 10.1051/parasite/2010174363
ISSN: 1252-607X
PubMed: 21275244
WoS: 000286649200014
Scopus: 2-s2.0-78650954317
Institucija/grupa
Institut za medicinska istraživanjaTY - JOUR AU - Radulović, Željko AU - Milutinović, Marija AU - Tomanović, Snežana AU - Mulenga, Albert PY - 2010 UR - http://rimi.imi.bg.ac.rs/handle/123456789/274 AB - We have previously found apparent differences in Gpdh allele frequences between borrelia infected and uninfected Ixodes riotous 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. PB - EDP Sciences S A, Les Ulis Cedex A T2 - Parasite T1 - Exon variability of gene encoding glycerol-3-phosphate dehydrogenase of ixodes ricinus ticks EP - 368 IS - 4 SP - 363 VL - 17 DO - 10.1051/parasite/2010174363 ER -
@article{ author = "Radulović, Željko and Milutinović, Marija and Tomanović, Snežana and Mulenga, Albert", year = "2010", abstract = "We have previously found apparent differences in Gpdh allele frequences between borrelia infected and uninfected Ixodes riotous 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.", publisher = "EDP Sciences S A, Les Ulis Cedex A", journal = "Parasite", title = "Exon variability of gene encoding glycerol-3-phosphate dehydrogenase of ixodes ricinus ticks", pages = "368-363", number = "4", volume = "17", doi = "10.1051/parasite/2010174363" }
Radulović, Ž., Milutinović, M., Tomanović, S.,& Mulenga, A.. (2010). Exon variability of gene encoding glycerol-3-phosphate dehydrogenase of ixodes ricinus ticks. in Parasite EDP Sciences S A, Les Ulis Cedex A., 17(4), 363-368. https://doi.org/10.1051/parasite/2010174363
Radulović Ž, Milutinović M, Tomanović S, Mulenga A. Exon variability of gene encoding glycerol-3-phosphate dehydrogenase of ixodes ricinus ticks. in Parasite. 2010;17(4):363-368. doi:10.1051/parasite/2010174363 .
Radulović, Željko, Milutinović, Marija, Tomanović, Snežana, Mulenga, Albert, "Exon variability of gene encoding glycerol-3-phosphate dehydrogenase of ixodes ricinus ticks" in Parasite, 17, no. 4 (2010):363-368, https://doi.org/10.1051/parasite/2010174363 . .