Literature DB >> 27038826

A single R36Q mutation in the matrix protein of pigeon paramyxovirus type 1 reduces virus replication and shedding in pigeons.

Haixu Xu1,2, Qingqing Song1,2, Jie Zhu3, Jiajia Liu1,2, Xin Cheng1,2, Shunlin Hu1,2, Shuang Wu4, Xiaoquan Wang1,2, Xiaowen Liu1,2, Xiufan Liu5,6.   

Abstract

Pigeon paramyxovirus type 1 (PPMV-1) is considered an antigenic and variant of avian paramyxovirus type 1 (APMV-1) that has adapted to pigeons as hosts. However, how this host-specific adaption of PPMV-1 is related to its biological characteristics is unknown. In this study, seven unique amino acids in PPMV-1 that are not present in other APMV-1 strains (n = 39 versus n = 106) were identified. R36 of the M protein was found to be not only a unique amino acid but also a positive-selection site. To investigate the role of R36 in host adaptation, a recombinant PPMV-1 with R36Q mutation was constructed. Our results indicated that the an R36Q mutation significantly attenuates pathogenicity in chickens, viral growth in both chicken embryo fibroblasts (CEFs) and pigeon embryo fibroblasts (PEFs), and virus replication and shedding in pigeons in comparison with the wild-type virus, suggesting that R36 is a key residue that evolved during the adaptation of PPMV-1 in pigeons.

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Keywords:  Host-specific adaptation; Matrix protein; Pigeon paramyxovirus type 1; R36; Unique amino acid

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Year:  2016        PMID: 27038826     DOI: 10.1007/s00705-016-2847-2

Source DB:  PubMed          Journal:  Arch Virol        ISSN: 0304-8608            Impact factor:   2.574


  1 in total

1.  Chicken bromodomain-containing protein 2 interacts with the Newcastle disease virus matrix protein and promotes viral replication.

Authors:  Zhiqiang Duan; Yifan Han; Lei Zhou; Chao Yuan; Yanbi Wang; Caiqin Zhao; Hong Tang; Jiaqi Chen
Journal:  Vet Res       Date:  2020-09-22       Impact factor: 3.683

  1 in total

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