NDLI: Selection and characterization of human respiratory syncytial virus escape mutants resistant to a polyclonal antiserum raised against the F protein

Content Provider	Springer Nature Link
Author	Tomé, Lorena Frabasile, Sandra Candia, Claudia Pittini, Alvaro Farina, Natalia Melero, José Antonio Arbiza, Juan
Copyright Year	2012
Abstract	A human respiratory syncytial virus (HRSV) neutralization escape mutant was obtained after 56 serial passages in the presence of a polyclonal antiserum raised against the F protein. Nucleotide sequence analysis of this escape mutant virus revealed two amino acid substitutions: Asn268Ile and Val533Met. When this virus was allowed to grow in the absence of the anti-F polyclonal serum, only the mutation Asn268Ile was stably maintained. Both the double and single escape mutant viruses lost reactivity with mAbs belonging to antigenic site II of the fusion protein of RSV. Mutation Asn268Ile has already been reported in RS viruses that are resistant to mAbs 47F and 11 and palivizumab (PZ). We have thus identified a novel mutation (Val533Met) in the transmembrane domain of the F protein that was selected under immune pressure.
Starting Page	1071
Ending Page	1080
Page Count	10
File Format	PDF
ISSN	03048608
Journal	Archives of Virology
Volume Number	157
Issue Number	6
e-ISSN	14328798
Language	English
Publisher	Springer Vienna
Publisher Date	2012-03-14
Publisher Place	Vienna
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Virology Infectious Diseases Medical Microbiology
Content Type	Text
Resource Type	Article
Subject	Virology Medicine

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Selection and characterization of human respiratory syncytial virus escape mutants resistant to a polyclonal antiserum raised against the F protein