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Vol.63 (2017) >

Please use this identifier to cite or link to this item: http://ir.fmu.ac.jp/dspace/handle/123456789/665

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Title: Neutralizing epitopes of RSV and palivizumab resistance in Japan
Authors: Hashimoto, Koichi
Hosoya, Mitsuaki
Affiliation: 小児科学講座
Source title: Fukushima Journal of Medical Science
Volume: 63
Issue: 3
Start page: 127
End page: 134
Issue Date: 2017
Abstract: Respiratory Syncytial Virus (RSV) is one of the most important viral pathogen related to acute lower respiratory infection in young children. The virus surface envelope contains the G, F, and SH proteins as spike proteins. The F protein is considered to be a major antigenic target for the neutralizing (NT) epitope as only the F protein is essential for cell infection among the three viral envelope proteins, and it is more highly conserved than the G protein. Recently, four antigenic targets related to NT activity have been reported;site I, site II, site IV, and site zero (0). Site II is the target for palivizumab used throughout the world to suppress severe RSV infection as passive immunity in high-risk children since 1998. Under the recent conditions in which indications for palivizumab administered subjects are being expanded, palivizumab-resistant mutations have been confirmed overseas in children with RSV infection, although they remain infrequent. Therefore, continuous genetic analysis of the palivizumab-binding region of the F protein is necessary. In addition, as vaccine development progresses, RSV infection control is expected to improve greatly over the next decade.
Publisher: The Fukushima Society of Medical Science
Publisher (Alternative foam): 福島医学会
language: eng
URI: http://ir.fmu.ac.jp/dspace/handle/123456789/665
Full text URL: http://ir.fmu.ac.jp/dspace/bitstream/123456789/665/1/FksmJMedSci_63_p127.pdf
ISSN: 0016-2590
DOI: 10.5387/fms.2017-09
PubMed ID: 28867684
Related Page: https://doi.org/10.5387/fms.2017-09
Rights: © 2017 The Fukushima Society of Medical Science
Appears in Collections:Vol.63 (2017)

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FksmJMedSci_63_p127.pdf134.81 kBAdobe PDFDownload

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