tetano
Editor, Senior Moderator
Virology. 2013 Dec;447(1-2):233-9. doi: 10.1016/j.virol.2013.09.013. Epub 2013 Oct 4.
Pleiotropic effects of hemagglutinin amino acid substitutions of H5 influenza escape mutants.
Rudneva IA, Timofeeva TA, Ignatieva AV, Shilov AA, Krylov PS, Ilyushina NA, Kaverin NV.
Source
D.I. Ivanovsky Institute of Virology, 123098 Moscow, Russia.
Abstract
In the present study we assessed pleiotropic characteristics of the antibody-selected mutations. We examined pH optimum of fusion, temperatures of HA heat inactivation, and in vitro and in vivo replication kinetics of the previously obtained influenza H5 escape mutants. Our results showed that HA1 N142K mutation significantly lowered the pH of fusion optimum. Mutations of the escape mutants located in the HA lateral loop significantly affected H5 HA thermostability (P<0.05). HA changes at positions 131, 144, 145, and 156 and substitutions at positions 131, 142, 145, and 156 affected the replicative ability of H5 escape mutants in vitro and in vivo, respectively. Overall, a co-variation between antigenic specificity and different HA phenotypic properties has been demonstrated. We believe that the monitoring of pleiotropic effects of the HA mutations found in H5 escape mutants is essential for accurate prediction of mutants with pandemic potential.
? 2013 Elsevier Inc. All rights reserved.
KEYWORDS:
H5 hemagglutinin, Influenza escape mutants, Pleiotropic antibody-neutralizing mutations
PMID:
24210119
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/24210119
Pleiotropic effects of hemagglutinin amino acid substitutions of H5 influenza escape mutants.
Rudneva IA, Timofeeva TA, Ignatieva AV, Shilov AA, Krylov PS, Ilyushina NA, Kaverin NV.
Source
D.I. Ivanovsky Institute of Virology, 123098 Moscow, Russia.
Abstract
In the present study we assessed pleiotropic characteristics of the antibody-selected mutations. We examined pH optimum of fusion, temperatures of HA heat inactivation, and in vitro and in vivo replication kinetics of the previously obtained influenza H5 escape mutants. Our results showed that HA1 N142K mutation significantly lowered the pH of fusion optimum. Mutations of the escape mutants located in the HA lateral loop significantly affected H5 HA thermostability (P<0.05). HA changes at positions 131, 144, 145, and 156 and substitutions at positions 131, 142, 145, and 156 affected the replicative ability of H5 escape mutants in vitro and in vivo, respectively. Overall, a co-variation between antigenic specificity and different HA phenotypic properties has been demonstrated. We believe that the monitoring of pleiotropic effects of the HA mutations found in H5 escape mutants is essential for accurate prediction of mutants with pandemic potential.
? 2013 Elsevier Inc. All rights reserved.
KEYWORDS:
H5 hemagglutinin, Influenza escape mutants, Pleiotropic antibody-neutralizing mutations
PMID:
24210119
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/24210119