Antigenic sites variation of fusion protein of respiratory syncytial virus isolated from children with acute respiratory tract infection in Beijing area
10.3760/cma.j.issn.1003-9279.2015.05.006
- VernacularTitle:北京地区急性呼吸道感染儿童RSV F蛋白抗原位点变异分析
- Author:
Xiangpeng CHEN
1
;
Feng ZHANG
;
Jiayun GUO
;
Yun ZHU
;
Chunyan LIU
;
Zhengde XIE
Author Information
1. 100045北京,首都医科大学附属北京儿童医院、北京市儿科研究所,儿科学国家重点学科,教育部儿科重大疾病研究重点实验室
- Keywords:
Respiratory syncytial virus;
Fusion protein;
Antigenic sites;
Variation;
Palivizumab
- From:
Chinese Journal of Experimental and Clinical Virology
2015;29(5):409-412
- CountryChina
- Language:Chinese
-
Abstract:
Objective Respiratory Syncytial Virus (RSV) fusion protein is an important transmembrane glycoprotein associated with virus infection and immunity.To clarify the genetic characteristics and antigenic sites variation in F protein,comprehensive analysis was performed with 61 RSV stains isolated in Beijing area.Methods The antigenic sites area of F protein gene of RSV was amplified by RT-PCR and sequenced.The Phylogenetic trees were constructed with MEGA program.The identity matrices and genetic sites variation were determined with Bioedit software.Results Pairwise nucleotide (amino acid) sequences identities were 95.9％-100％ (98.3％-100％) among 43 subtype A,97.5％ -100％ (98.7％-100％) among 18 subtype B,and 83.2％-84.9％ (93.1％-95.1％) between groups A and B,respectively.Phylogenetic analyses revealed that all the strains could be divided into two groups.Further,group A could be divided into 6 clusters,and group B could be divided into 3 clusters.There were 7 and 4 amino acid changes at group A and group B,respectively.Variations at antigenic site (Φ) were observed in amino residues 209 and 211.No more mutation was found on the antigenic sites area except the 276 (N→S) on palivizumab binding site.Conclusions The nucleotide and amino acid have high identity in F protein of Beijing RSV isolates except a few mutations.The F protein remains the potential candidate of RSV vaccine and molecular drugs.
