Mutations in the NDV fusion protein HR4 region decreased fusogenic activity due to failed protein expression

被引:0
|
作者
Liu, Yaqing [1 ,2 ]
Pan, Huazheng [1 ]
Wang, Hongwei [1 ]
Yuan, Yuan [1 ]
Cao, Fangfang [1 ]
Song, Wei [1 ]
Wang, Zhiyu [2 ,3 ]
机构
[1] Qingdao Univ, Dept Clin Lab, Affiliated Hosp, Qingdao 266000, Peoples R China
[2] Shandong Univ, Dept Virol, Sch Publ Hlth, Cheeloo Coll Med, Jinan 250014, Peoples R China
[3] Shandong Univ, Cheeloo Coll Med, Jinan 250014, Peoples R China
基金
中国国家自然科学基金;
关键词
NDV; Fusion protein; Heptad repeat; Fusogenic activity; Protein expression; DISEASE-VIRUS FUSION; SINGLE AMINO-ACID; F-PROTEIN; HEPTAD REPEAT; CLEAVAGE SITE; GLYCOPROTEIN; ACTIVATION; ATTACHMENT; PROMOTION; RESIDUES;
D O I
10.1016/j.micpath.2024.106713
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Newcastle disease virus (NDV) is the pathogen of a zoonosis that is primarily transmitted by poultry and has severe infectivity and a high fatality rate. Many studies have focused on the role of the NDV fusion (F) protein in the cell-cell membrane fusion process. However, little attention has been given to the heptad repeat region, HR4, which is located in the NDV F2 subunit. Here, site-directed mutants were constructed to study the function of the NDV F protein HR4 region and identify the key amino acids in this region. Nine conserved amino acids were substituted with alanine or the corresponding amino acid of other aligned paramyxoviruses. The desired mutants were examined for changes in fusogenic activity through three kinds of membrane fusion assays and expression and proteolysis through IFA, FACS and WB. The results showed that when conserved amino acids (L81, Y84, L88, L91, L92, P94, L95 and I99) were replaced with alanine, the fusogenic activity of the F protein was abolished, possibly because of failed protein expression not only on the cell surface but also inside cells. These data indicated that the conserved amino acids above in NDV F HR4 are critical for normal protein synthesis and expression, possibly for the stability of the F protein monomer, formation of trimer and conformational changes.
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页数:10
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