Giuseppe
Emeritus
[Source: PLoS ONE, full text: (LINK). Abstract, edited.]
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The Evolutionary Pattern of Glycosylation Sites in Influenza Virus (H5N1) Hemagglutinin and Neuraminidase
Wentian Chen<SUP>1</SUP>, Yaogang Zhong<SUP>1</SUP>, Yannan Qin<SUP>1</SUP>, Shisheng Sun<SUP>2</SUP>, Zheng Li<SUP>1</SUP><SUP>*</SUP>
<SUP></SUP>
1 Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an, People's Republic of China, 2 Department of Pathology, Clinical Chemistry Division, Johns Hopkins University, Baltimore, Maryland, United States of America
Abstract
Two glycoproteins, hemagglutinin (HA) and neuraminidase (NA), on the surface of influenza viruses play crucial roles in transfaunation, membrane fusion and the release of progeny virions. To explore the distribution of N-glycosylation sites (glycosites) in these two glycoproteins, we collected and aligned the amino acid sequences of all the HA and NA subtypes. Two glycosites were located at HA0 cleavage sites and fusion peptides and were strikingly conserved in all HA subtypes, while the remaining glycosites were unique to their subtypes. Two to four conserved glycosites were found in the stalk domain of NA, but these are affected by the deletion of specific stalk domain sequences. Another highly conserved glycosite appeared at the top center of tetrameric global domain, while the others glycosites were distributed around the global domain. Here we present a detailed investigation of the distribution and the evolutionary pattern of the glycosites in the envelope glycoproteins of IVs, and further focus on the H5N1 virus and conclude that the glycosites in H5N1 have become more complicated in HA and less influential in NA in the last five years.
Citation: Chen W, Zhong Y, Qin Y, Sun S, Li Z (2012) The Evolutionary Pattern of Glycosylation Sites in Influenza Virus (H5N1) Hemagglutinin and Neuraminidase. PLoS ONE 7(11): e49224. doi:10.1371/journal.pone.0049224
Editor: Earl G. Brown, University of Ottawa, Canada
Received: June 11, 2012; Accepted: October 4, 2012; Published: November 1, 2012
Copyright: ? 2012 Chen et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Funding: This work was supported by the International S&T (Science and Technology) Cooperation Program (2009DFA32730) and the Key Science and Technology Program (2010K12- 02(5)) of the Shaanxi Province of China. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
Competing interests: The authors have declared that no competing interests exist.
* E-mail: zhengli@nwu.edu.cn
-Wentian Chen<SUP>1</SUP>, Yaogang Zhong<SUP>1</SUP>, Yannan Qin<SUP>1</SUP>, Shisheng Sun<SUP>2</SUP>, Zheng Li<SUP>1</SUP><SUP>*</SUP>
<SUP></SUP>
1 Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an, People's Republic of China, 2 Department of Pathology, Clinical Chemistry Division, Johns Hopkins University, Baltimore, Maryland, United States of America
Abstract
Two glycoproteins, hemagglutinin (HA) and neuraminidase (NA), on the surface of influenza viruses play crucial roles in transfaunation, membrane fusion and the release of progeny virions. To explore the distribution of N-glycosylation sites (glycosites) in these two glycoproteins, we collected and aligned the amino acid sequences of all the HA and NA subtypes. Two glycosites were located at HA0 cleavage sites and fusion peptides and were strikingly conserved in all HA subtypes, while the remaining glycosites were unique to their subtypes. Two to four conserved glycosites were found in the stalk domain of NA, but these are affected by the deletion of specific stalk domain sequences. Another highly conserved glycosite appeared at the top center of tetrameric global domain, while the others glycosites were distributed around the global domain. Here we present a detailed investigation of the distribution and the evolutionary pattern of the glycosites in the envelope glycoproteins of IVs, and further focus on the H5N1 virus and conclude that the glycosites in H5N1 have become more complicated in HA and less influential in NA in the last five years.
Citation: Chen W, Zhong Y, Qin Y, Sun S, Li Z (2012) The Evolutionary Pattern of Glycosylation Sites in Influenza Virus (H5N1) Hemagglutinin and Neuraminidase. PLoS ONE 7(11): e49224. doi:10.1371/journal.pone.0049224
Editor: Earl G. Brown, University of Ottawa, Canada
Received: June 11, 2012; Accepted: October 4, 2012; Published: November 1, 2012
Copyright: ? 2012 Chen et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Funding: This work was supported by the International S&T (Science and Technology) Cooperation Program (2009DFA32730) and the Key Science and Technology Program (2010K12- 02(5)) of the Shaanxi Province of China. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
Competing interests: The authors have declared that no competing interests exist.
* E-mail: zhengli@nwu.edu.cn
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