A homolog of glyceraldehyde-3-phosphate dehydrogenase from Riemerella anatipestifer is an extracellular protein and exhibits biological activity
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Ji-ye Gao, Cui-lian Ye, Li-li Zhu, Zhi-ying Tian, Zhi-bang Yang. A homolog of glyceraldehyde-3-phosphate dehydrogenase from Riemerella anatipestifer is an extracellular protein and exhibits biological activity[J]. Journal of Zhejiang University Science B, 2014, 15(9): 776-787.
@article{title="A homolog of glyceraldehyde-3-phosphate dehydrogenase from Riemerella anatipestifer is an extracellular protein and exhibits biological activity",
author="Ji-ye Gao, Cui-lian Ye, Li-li Zhu, Zhi-ying Tian, Zhi-bang Yang",
journal="Journal of Zhejiang University Science B",
volume="15",
number="9",
pages="776-787",
year="2014",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.B1400023"
}
%0 Journal Article
%T A homolog of glyceraldehyde-3-phosphate dehydrogenase from Riemerella anatipestifer is an extracellular protein and exhibits biological activity
%A Ji-ye Gao
%A Cui-lian Ye
%A Li-li Zhu
%A Zhi-ying Tian
%A Zhi-bang Yang
%J Journal of Zhejiang University SCIENCE B
%V 15
%N 9
%P 776-787
%@ 1673-1581
%D 2014
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.B1400023
TY - JOUR
T1 - A homolog of glyceraldehyde-3-phosphate dehydrogenase from Riemerella anatipestifer is an extracellular protein and exhibits biological activity
A1 - Ji-ye Gao
A1 - Cui-lian Ye
A1 - Li-li Zhu
A1 - Zhi-ying Tian
A1 - Zhi-bang Yang
J0 - Journal of Zhejiang University Science B
VL - 15
IS - 9
SP - 776
EP - 787
%@ 1673-1581
Y1 - 2014
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.B1400023
Abstract:
Riemerella anatipestifer is the causative agent of septicemia anserum exsudativa in ducks. Its pathogenesis and virulence factors are still unclear. The glycolytic enzyme, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), an anchorless and multifunctional protein on the surface of several pathogenic microorganisms, is involved in virulence and adhesion. Whether homologs of GAPDH exist, and display similar characteristics in R. anatipestifer (RaGAPDH) has not been determined. In our research, the RaGAPDH activity from various R. anatipestifer isolates was confirmed. Twenty-two gapdh genes from genomic DNA of R. anatipestifer isolates were cloned and sequenced for phylogenetic analysis. The distribution of RaGAPDH in R. anatipestifer CZ2 strain was confirmed by antisera to recombinant RaGAPDH. The ability of purified RaGAPDH to bind host proteins was analyzed by solid-phase ligand-binding assay. Results revealed that all R. anatipestifer isolates showed different levels of GAPDH activity except four strains, which contained a gapdh-like gene. The gapdh of R. anatipestifer, which is located phylogenetically in the same branch as enterohemorrhagic Escherichia coli (EHEC), belonged to class I GAPDH, and encoded a 36.7-kDa protein. All RaGAPDH-encoding gene sequences from field isolates of R. anatipestifer displayed 100% homology. The RaGAPDH localized on the extracellular membrane of several R. anatipestifer strains. Further, it was released into the culture medium, and exhibited GAPDH enzyme activity. We also confirmed the binding of RaGAPDH to plasminogen and fibrinogen. These results demonstrated that GAPDH was present in R. anatipestifer, although not in all strains, and that RaGAPDH might contribute to the microorganism’s virulence.
Full Text:
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CLC number: Q936; S85
On-line Access: 2024-08-27
Received: 2023-10-17
Revision Accepted: 2024-05-08
Crosschecked: 2014-08-21
Cited: 1
Clicked: 13776
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