Infectivity studies of influenza virus hemagglutinin receptor binding site mutants in mice

被引:21
作者
Meisner, Jeffrey
Szretter, Kristy J. [2 ]
Bradley, Konrad C.
Langley, William A.
Li, Zhu-Nan
Lee, Byeong-Jae
Thoennes, Sudha
Martin, Javier [3 ]
Skehel, John J. [4 ]
Russell, Rupert J. [5 ]
Katz, Jacqueline M. [2 ]
Steinhauer, David A. [1 ]
机构
[1] Emory Univ, Sch Med, Dept Microbiol & Immunol, Atlanta, GA 30322 USA
[2] CDC, Influenza Branch MS G16, Atlanta, GA 30333 USA
[3] Natl Inst Biol Stand & Controls, Blanche Lane, Div Virol, Potters Bar EN6 3QG, Herts, England
[4] Natl Inst Med Res, London NW7 1AA, England
[5] Univ St Andrews, Sch Biol, St Andrews KY16 9ST, Fife, Scotland
基金
英国医学研究理事会;
关键词
D O I
10.1128/JVI.01958-07
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The replicative properties of influenza virus hemagglutinin (RA) mutants with altered receptor binding characteristics were analyzed following intranasal inoculation of mice. Among the mutants examined was a virus containing a Y98F substitution at a conserved position in the receptor binding site that leads to a 20-fold reduction in binding. This mutant can replicate as well as wild-type (WT) virus in MDCK cells and in embryonated chicken eggs but is highly attenuated in mice, exhibiting titers in lungs more than 1,000-fold lower than those of the WT. The capacity of the Y98F mutant to induce antibody responses and the structural locations of HA reversion mutations are examined.
引用
收藏
页码:5079 / 5083
页数:5
相关论文
共 40 条
[1]   Inhibition of release of lentivirus particles with incorporated human influenza virus haemagglutinin by binding to sialic acid-containing cellular receptors [J].
Bosch, V ;
Kramer, B ;
Pfeiffer, T ;
Stärck, L ;
Steinhauer, DA .
JOURNAL OF GENERAL VIROLOGY, 2001, 82 :2485-2494
[2]  
BRANDLI AW, 1988, J BIOL CHEM, V263, P16283
[3]   Large-plaque mutants of sindbis virus show reduced binding to heparan sulfate, heightened viremia, and slower clearance from the circulation [J].
Byrnes, AP ;
Griffin, DE .
JOURNAL OF VIROLOGY, 2000, 74 (02) :644-651
[4]   Glycan topology determines human adaptation of avian H5N1 virus hemagglutinin [J].
Chandrasekaran, Aarthi ;
Srinivasan, Aravind ;
Raman, Rahul ;
Viswanathan, Karthik ;
Raguram, S. ;
Tumpey, Terrence M. ;
Sasisekharan, V. ;
Sasisekharan, Ram .
NATURE BIOTECHNOLOGY, 2008, 26 (01) :107-113
[5]   RECEPTOR SPECIFICITY IN HUMAN, AVIAN, AND EQUINE H2 AND H3 INFLUENZA-VIRUS ISOLATES [J].
CONNOR, RJ ;
KAWAOKA, Y ;
WEBSTER, RG ;
PAULSON, JC .
VIROLOGY, 1994, 205 (01) :17-23
[6]   THE RECEPTOR-BINDING AND MEMBRANE-FUSION PROPERTIES OF INFLUENZA-VIRUS VARIANTS SELECTED USING ANTI-HEMAGGLUTININ MONOCLONAL-ANTIBODIES [J].
DANIELS, RS ;
JEFFRIES, S ;
YATES, P ;
SCHILD, GC ;
ROGERS, GN ;
PAULSON, JC ;
WHARTON, SA ;
DOUGLAS, AR ;
SKEHEL, JJ ;
WILEY, DC .
EMBO JOURNAL, 1987, 6 (05) :1459-1465
[7]   Effects of egg-adaptation on the receptor-binding properties of human influenza A and B viruses [J].
Gambaryan, AS ;
Robertson, JS ;
Matrosovich, MN .
VIROLOGY, 1999, 258 (02) :232-239
[8]   Specification of receptor-binding phenotypes of influenza virus isolates from different hosts using synthetic sialylglycopolymers: Non-egg-adapted human H1 and H3 influenza A and influenza B viruses share a common high binding affinity for 6'-sialyl(N-acetyllactosamine) [J].
Gambaryan, AS ;
Tuzikov, AB ;
Piskarev, VE ;
Yamnikova, SS ;
Lvov, DK ;
Robertson, JS ;
Bovin, NV ;
Matrosovich, MN .
VIROLOGY, 1997, 232 (02) :345-350
[9]   The structure and receptor binding properties of the 1918 influenza hemagglutinin [J].
Gamblin, SJ ;
Haire, LF ;
Russell, RJ ;
Stevens, DJ ;
Xiao, B ;
Ha, Y ;
Vasisht, N ;
Steinhauer, DA ;
Daniels, RS ;
Elliot, A ;
Wiley, DC ;
Skehel, JJ .
SCIENCE, 2004, 303 (5665) :1838-1842
[10]   Effective replication of human influenza viruses in mice lacking a major α2,6 sialyltransferase [J].
Glaser, Laurel ;
Conenello, Gina ;
Paulson, James ;
Palese, Peter .
VIRUS RESEARCH, 2007, 126 (1-2) :9-18