1992
DOI: 10.1016/0042-6822(92)90683-g
|View full text |Cite
|
Sign up to set email alerts
|

Location of neutralizing epitopes on the hemagglutinin-esterase protein of influenza C virus

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

1
22
0

Year Published

1994
1994
2020
2020

Publication Types

Select...
7
2

Relationship

1
8

Authors

Journals

citations
Cited by 28 publications
(23 citation statements)
references
References 39 publications
1
22
0
Order By: Relevance
“…These observations suggest that the production of antigenic variants by immune selection has not occurred for the last 3 decades. This finding is well comparable with our previous indication that HE protein might no longer be able to evolve in response to antibody pressure because of a high degree of functional constraint on the change of its immunodominant region, which is near the receptor-binding site (15,21). On the other hand, as shown in Fig.…”
Section: Discussionsupporting
confidence: 81%
“…These observations suggest that the production of antigenic variants by immune selection has not occurred for the last 3 decades. This finding is well comparable with our previous indication that HE protein might no longer be able to evolve in response to antibody pressure because of a high degree of functional constraint on the change of its immunodominant region, which is near the receptor-binding site (15,21). On the other hand, as shown in Fig.…”
Section: Discussionsupporting
confidence: 81%
“…Although there are no sites under significant positive selection, some sites responsible for antigenicity [11] showed positive selection pressure (Supplementary Table S2 and positive blue bars in Figure 5). Additionally, other positions in antigenic sites showed negative selection pressure (Supplementary Table S2 and negative blue bars in Figure 5).…”
Section: Resultsmentioning
confidence: 99%
“…The fourth segment of the viral genome encodes hemagglutinin-esterase (HE) glycoprotein [9], which determines the major antigenicity of the virus and has a variety of functions in the viral replication cycle. At least nine antigenic sites (A-1 to A-5 and B-1 to B-4) of the HE glycoproteins are proposed; of them, amino acid positions responsible for four antigenic sites have been identified [10,11,12]. In addition, glycosylation of the proteins also affects the virus’ antigenicity [10].…”
Section: Introductionmentioning
confidence: 99%
“…However, ICV HEF binds to N-acetyl-9-O-acetylneuraminic acid rather than to N-acetyl-neuraminic acid for influenza A and B viruses [36]. HEF is the major target for host neutralizing antibodies, which appear to bind to epitopes near the receptor-binding site and the esterase site [37][38][39][40][41][42]. Human CD8+ T cells recognize epitopes of ICV internal proteins, some of which are conserved in IAV and IBV [43].…”
Section: Virus Structurementioning
confidence: 99%