Abstract
MALDI-TOF MS and N-terminal amino acid sequencing allowed us to identify several fragments of the C-terminal peptide of Influenza A hemagglutinin (HA) containing transmembrane domains (TMD). These fragments were detected in the organic phase of chloroform-methanol extracts from bromelain-treated virus particles. Heterogeneous fatty acylation of the C-terminus was revealed. Tritium bombardment technique might open an opportunity for 3D structural investigation of the HA TMD in situ.
Keywords: influenza a virus, hemagglutinin, fatty acylation, transmembrane domain
Protein & Peptide Letters
Title: Influenza a Hemagglutinin C-terminal Anchoring Peptide: Identification and Mass Spectrometric Study
Volume: 11 Issue: 4
Author(s): Larisa V. Kordyukova, Aleksander L. Ksenofontov, Marina V. Serebryakova, Tatyana V. Ovchinnikova, Natalija V. Fedorova, Valeria T. Ivanova and Ludmila A. Baratova
Affiliation:
Keywords: influenza a virus, hemagglutinin, fatty acylation, transmembrane domain
Abstract: MALDI-TOF MS and N-terminal amino acid sequencing allowed us to identify several fragments of the C-terminal peptide of Influenza A hemagglutinin (HA) containing transmembrane domains (TMD). These fragments were detected in the organic phase of chloroform-methanol extracts from bromelain-treated virus particles. Heterogeneous fatty acylation of the C-terminus was revealed. Tritium bombardment technique might open an opportunity for 3D structural investigation of the HA TMD in situ.
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Cite this article as:
Kordyukova V. Larisa, L. Ksenofontov Aleksander, V. Serebryakova Marina, V. Ovchinnikova Tatyana, V. Fedorova Natalija, T. Ivanova Valeria and A. Baratova Ludmila, Influenza a Hemagglutinin C-terminal Anchoring Peptide: Identification and Mass Spectrometric Study, Protein & Peptide Letters 2004; 11 (4) . https://dx.doi.org/10.2174/0929866043406850
DOI https://dx.doi.org/10.2174/0929866043406850 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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