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Viruses 2015, 7(12), 6458-6475; doi:10.3390/v7122950

Two Cytoplasmic Acylation Sites and an Adjacent Hydrophobic Residue, but No Other Conserved Amino Acids in the Cytoplasmic Tail of HA from Influenza A Virus Are Crucial for Virus Replication

1
Institute of Virology, Faculty of Veterinary Medicine, Freie Universität Berlin, 14163 Berlin, Germany
2
Robert Koch Institute, Advanced Light and Electron Microscopy (ZBS4), Nordufer 20, 13353 Berlin, Germany
3
A.N. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, Russia
4
I.I. Mechnikov Research Institute of Vaccines and Sera, Russian Academy of Medical Sciences, 105064 Moscow, Russia
5
Department of Bioengineering and Bioinformatics, Lomonosov Moscow State University, 119991 Moscow, Russia
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editor: Andrew Mehle
Received: 11 October 2015 / Revised: 24 November 2015 / Accepted: 3 December 2015 / Published: 8 December 2015
(This article belongs to the Section Animal Viruses)
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Abstract

Recruitment of the matrix protein M1 to the assembly site of the influenza virus is thought to be mediated by interactions with the cytoplasmic tail of hemagglutinin (HA). Based on a comprehensive sequence comparison of all sequences present in the database, we analyzed the effect of mutating conserved residues in the cytosol-facing part of the transmembrane region and cytoplasmic tail of HA (A/WSN/33 (H1N1) strain) on virus replication and morphology of virions. Removal of the two cytoplasmic acylation sites and substitution of a neighboring isoleucine by glutamine prevented rescue of infectious virions. In contrast, a conservative exchange of the same isoleucine, non-conservative exchanges of glycine and glutamine, deletion of the acylation site at the end of the transmembrane region and shifting it into the tail did not affect virus morphology and had only subtle effects on virus growth and on the incorporation of M1 and Ribo-Nucleoprotein Particles (RNPs). Thus, assuming that essential amino acids are conserved between HA subtypes we suggest that, besides the two cytoplasmic acylation sites (including adjacent hydrophobic residues), no other amino acids in the cytoplasmic tail of HA are indispensable for virus assembly and budding. View Full-Text
Keywords: influenza virus; assembly; hemagglutinin; cytoplasmic tail; transmembrane region; acylation; palmitoylation; M1; J0101 influenza virus; assembly; hemagglutinin; cytoplasmic tail; transmembrane region; acylation; palmitoylation; M1; J0101
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MDPI and ACS Style

Siche, S.; Brett, K.; Möller, L.; Kordyukova, L.V.; Mintaev, R.R.; Alexeevski, A.V.; Veit, M. Two Cytoplasmic Acylation Sites and an Adjacent Hydrophobic Residue, but No Other Conserved Amino Acids in the Cytoplasmic Tail of HA from Influenza A Virus Are Crucial for Virus Replication. Viruses 2015, 7, 6458-6475.

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