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Basic Characteristics of Mutations
|
|
Mutation Site
|
E125D |
|
Mutation Site Sentence
|
Table 2. Mutations identified in passaged viruses |
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Mutation Level
|
Amino acid level |
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Mutation Type
|
Nonsynonymous substitution |
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Gene/Protein/Region
|
NS1 |
|
Standardized Encoding Gene
|
NS
|
|
Genotype/Subtype
|
H1N1 |
|
Viral Reference
|
A/Netherlands/602/2009 (H1N1)
|
|
Functional Impact and Mechanisms
|
|
Disease
|
Influenza A
Influenza B
|
|
Immune
|
- |
|
Target Gene
|
-
|
|
Clinical and Epidemiological Correlations
|
|
Clinical Information
|
- |
|
Treatment
|
- |
|
Location
|
- |
|
Literature Information
|
|
PMID
|
35446141
|
|
Title
|
Novel Epitopes of the Influenza Virus N1 Neuraminidase Targeted by Human Monoclonal Antibodies
|
|
Author
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Kirkpatrick Roubidoux E,Sano K,McMahon M,Carreno JM,Capuano C,Jiang K,Simon V,van Bakel H,Wilson P,Krammer F
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Journal
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Journal of virology
|
|
Journal Info
|
2022 May 11;96(9):e0033222
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|
Abstract
|
Influenza virus neuraminidase (NA)-targeting antibodies are an independent correlate of protection against influenza. Antibodies against the NA act by blocking enzymatic activity, preventing virus release and transmission. As we advance the development of improved influenza virus vaccines that incorporate standard amounts of NA antigen, it is important to identify the antigenic targets of human monoclonal antibodies (mAbs). Here, we describe escape mutants generated by serial passage of A/Netherlands/602/2009 (H1N1)pdm09 in the presence of human anti-N1 mAbs. We observed escape mutations on the head domain of the N1 protein around the enzymatic site (S364N, N369T, and R430Q) and also detected escape mutations located on the sides and bottom of the NA (N88D, N270D, and Q313K/R). This work increases our understanding of how human antibody responses target the N1 protein. IMPORTANCE As improved influenza virus vaccines are being developed, the influenza virus neuraminidase (NA) is becoming an important new target for immune responses. By identifying novel epitopes of anti-NA antibodies, we can improve vaccine design. Additionally, characterizing escape mutations in these epitopes aids in identifying NA antigenic drift in circulating viruses.
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|
Sequence Data
|
-
|