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Trypsin- and low pH-mediated fusogenicity of avian metapneumovirus fusion proteins is determined by residues at positions 100, 101 and 294
Avian metapneumovirus (aMPV) and human metapneumovirus (hMPV) are members of the genus Metapneumovirus in the subfamily Pneumovirinae. Metapneumovirus fusion (F) protein mediates the fusion of host cells with the virus membrane for infection. Trypsin- and/or low pH-induced membrane fusion is a strai...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4620442/ https://www.ncbi.nlm.nih.gov/pubmed/26498473 http://dx.doi.org/10.1038/srep15584 |
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author | Yun, Bingling Guan, Xiaolu Liu, Yongzhen Gao, Yanni Wang, Yongqiang Qi, Xiaole Cui, Hongyu Liu, Changjun Zhang, Yanping Gao, Li Li, Kai Gao, Honglei Gao, Yulong Wang, Xiaomei |
author_facet | Yun, Bingling Guan, Xiaolu Liu, Yongzhen Gao, Yanni Wang, Yongqiang Qi, Xiaole Cui, Hongyu Liu, Changjun Zhang, Yanping Gao, Li Li, Kai Gao, Honglei Gao, Yulong Wang, Xiaomei |
author_sort | Yun, Bingling |
collection | PubMed |
description | Avian metapneumovirus (aMPV) and human metapneumovirus (hMPV) are members of the genus Metapneumovirus in the subfamily Pneumovirinae. Metapneumovirus fusion (F) protein mediates the fusion of host cells with the virus membrane for infection. Trypsin- and/or low pH-induced membrane fusion is a strain-dependent phenomenon for hMPV. Here, we demonstrated that three subtypes of aMPV (aMPV/A, aMPV/B, and aMPV/C) F proteins promoted cell-cell fusion in the absence of trypsin. Indeed, in the presence of trypsin, only aMPV/C F protein fusogenicity was enhanced. Mutagenesis of the amino acids at position 100 and/or 101, located at a putative cleavage region in aMPV F proteins, revealed that the trypsin-mediated fusogenicity of aMPV F proteins is regulated by the residues at positions 100 and 101. Moreover, we demonstrated that aMPV/A and aMPV/B F proteins mediated cell-cell fusion independent of low pH, whereas the aMPV/C F protein did not. Mutagenesis of the residue at position 294 in the aMPV/A, aMPV/B, and aMPV/C F proteins showed that 294G played a critical role in F protein-mediated fusion under low pH conditions. These findings on aMPV F protein-induced cell-cell fusion provide new insights into the molecular mechanisms underlying membrane fusion and pathogenesis of aMPV. |
format | Online Article Text |
id | pubmed-4620442 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-46204422015-10-29 Trypsin- and low pH-mediated fusogenicity of avian metapneumovirus fusion proteins is determined by residues at positions 100, 101 and 294 Yun, Bingling Guan, Xiaolu Liu, Yongzhen Gao, Yanni Wang, Yongqiang Qi, Xiaole Cui, Hongyu Liu, Changjun Zhang, Yanping Gao, Li Li, Kai Gao, Honglei Gao, Yulong Wang, Xiaomei Sci Rep Article Avian metapneumovirus (aMPV) and human metapneumovirus (hMPV) are members of the genus Metapneumovirus in the subfamily Pneumovirinae. Metapneumovirus fusion (F) protein mediates the fusion of host cells with the virus membrane for infection. Trypsin- and/or low pH-induced membrane fusion is a strain-dependent phenomenon for hMPV. Here, we demonstrated that three subtypes of aMPV (aMPV/A, aMPV/B, and aMPV/C) F proteins promoted cell-cell fusion in the absence of trypsin. Indeed, in the presence of trypsin, only aMPV/C F protein fusogenicity was enhanced. Mutagenesis of the amino acids at position 100 and/or 101, located at a putative cleavage region in aMPV F proteins, revealed that the trypsin-mediated fusogenicity of aMPV F proteins is regulated by the residues at positions 100 and 101. Moreover, we demonstrated that aMPV/A and aMPV/B F proteins mediated cell-cell fusion independent of low pH, whereas the aMPV/C F protein did not. Mutagenesis of the residue at position 294 in the aMPV/A, aMPV/B, and aMPV/C F proteins showed that 294G played a critical role in F protein-mediated fusion under low pH conditions. These findings on aMPV F protein-induced cell-cell fusion provide new insights into the molecular mechanisms underlying membrane fusion and pathogenesis of aMPV. Nature Publishing Group 2015-10-26 /pmc/articles/PMC4620442/ /pubmed/26498473 http://dx.doi.org/10.1038/srep15584 Text en Copyright © 2015, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Yun, Bingling Guan, Xiaolu Liu, Yongzhen Gao, Yanni Wang, Yongqiang Qi, Xiaole Cui, Hongyu Liu, Changjun Zhang, Yanping Gao, Li Li, Kai Gao, Honglei Gao, Yulong Wang, Xiaomei Trypsin- and low pH-mediated fusogenicity of avian metapneumovirus fusion proteins is determined by residues at positions 100, 101 and 294 |
title | Trypsin- and low pH-mediated fusogenicity of avian metapneumovirus fusion proteins is determined by residues at positions 100, 101 and 294 |
title_full | Trypsin- and low pH-mediated fusogenicity of avian metapneumovirus fusion proteins is determined by residues at positions 100, 101 and 294 |
title_fullStr | Trypsin- and low pH-mediated fusogenicity of avian metapneumovirus fusion proteins is determined by residues at positions 100, 101 and 294 |
title_full_unstemmed | Trypsin- and low pH-mediated fusogenicity of avian metapneumovirus fusion proteins is determined by residues at positions 100, 101 and 294 |
title_short | Trypsin- and low pH-mediated fusogenicity of avian metapneumovirus fusion proteins is determined by residues at positions 100, 101 and 294 |
title_sort | trypsin- and low ph-mediated fusogenicity of avian metapneumovirus fusion proteins is determined by residues at positions 100, 101 and 294 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4620442/ https://www.ncbi.nlm.nih.gov/pubmed/26498473 http://dx.doi.org/10.1038/srep15584 |
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