Molecular Characterization of Respiratory Syncytial Virus in Children With Repeated Infections With Subgroup B in the Philippines
| Autor: | Raita Tamaki, Socorro Lupisan, Irene C Lirio, Leilanie P Batangan-Nacion, Michiko Okamoto, Ann Marie D Sandagon, Clyde Dapat, Hitoshi Oshitani, Mariko Saito-Obata, Mayuko Saito |
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| Rok vydání: | 2018 |
| Předmět: |
Male
0301 basic medicine G protein Philippines respiratory syncytial virus Respiratory Syncytial Virus Infections Biology Epitope Virus Cohort Studies Epitopes Major Articles and Brief Reports 03 medical and health sciences Antigen GTP-Binding Proteins Homologous chromosome Humans Immunology and Allergy Respiratory system Antigens Viral Respiratory Tract Infections repeated infection Gene Phylogeny chemistry.chemical_classification Infant RSV Virology Amino acid 030104 developmental biology Infectious Diseases Amino Acid Substitution chemistry Child Preschool Respiratory Syncytial Virus Human Acute Disease Viruses Female Viral Fusion Proteins |
| Zdroj: | The Journal of Infectious Diseases |
| ISSN: | 1537-6613 0022-1899 |
| Popis: | Background Human respiratory syncytial virus (RSV) is the leading cause of severe acute respiratory infection in infants and young children, which is characterized by repeated infections. However, the role of amino acid substitutions in repeated infections remains unclear. Hence, this study aimed to elucidate the genetic characteristics of RSV in children with repeated infections using molecular analyses of F and G genes. Methods We conducted a cohort study of children younger than 5 years in the Philippines. We collected nasopharyngeal swabs from children with acute respiratory symptoms and compared F and G sequences between initial and subsequent RSV infections. Results We examined 1802 children from May 2014 to January 2016 and collected 3471 samples. Repeated infections were observed in 25 children, including 4 with homologous RSV-B reinfections. Viruses from the 4 pairs of homologous reinfections had amino acid substitutions in the G protein mostly at O-glycosylation sites, whereas changes in the F protein were identified at antigenic sites V (L173S) and θ (Q209K), considered essential epitopes for the prefusion conformation of the F protein. Conclusions Amino acid substitutions in G and F proteins of RSV-B might have led to antigenic changes, potentially contributing to homologous reinfections observed in this study. The Q209K substitution in antigenic site θ and L173S substitution in antigenic site V of F protein and changes in O-linked glycosylation pattern in G protein of RSV-B may contribute to the homologous reinfections in children. |
| Databáze: | OpenAIRE |
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