Structure and dynamics of the proton-selective histidine and the gating tryptophan in an inward rectifying hybrid influenza B and A virus M2 proton channel.

Yanina Pankratova, Matthew J McKay, Chunlong Ma, Haozhou Tan, Jun Wang, Mei Hong

Abstract read

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Article in Physical chemistry chemical physics : PCCP, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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1citing papers in PubMed

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1 citing paper in PubMed.

Side Chain Structures of the Proton-Selective Histidine and Gating Tryptophan in Influenza BM2 Reveal Both Conservation and Variation of the Proton Conduction Mechanism.Biochemistry · 2025
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Authors and funding

6 authors.

Yanina PankratovaDepartment of Chemistry, Massachusetts Institute of Technology, 170 Albany Street, Cambridge, MA 02139, USA. meihong@mit.edu.ORCID http://orcid.org/0009-0003-8848-4213

Matthew J McKayDepartment of Chemistry, Massachusetts Institute of Technology, 170 Albany Street, Cambridge, MA 02139, USA. meihong@mit.edu.

Chunlong MaDepartment of Pharmacology and Toxicology, College of Pharmacy, University of Arizona, Tucson, Arizona, 85721, USA.

Haozhou TanDepartment of Medicinal Chemistry, Rutgers University, 160 Frelinghuysen Road, Piscataway, NJ 08854, USA.

Jun WangDepartment of Medicinal Chemistry, Rutgers University, 160 Frelinghuysen Road, Piscataway, NJ 08854, USA.ORCID http://orcid.org/0000-0002-4845-4621

Mei HongDepartment of Chemistry, Massachusetts Institute of Technology, 170 Albany Street, Cambridge, MA 02139, USA. meihong@mit.edu.ORCID http://orcid.org/0000-0001-5255-5858

Funding

Structures and Dynamics of Proton and Cation-Dependent Channels and TransportersR01GM088204 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI HONG, MEI · 2009 to 2024

$4.8M

NIGMS NIH HHS R01 GM088204

6 · The paper itself

Abstract

The M2 proteins of influenza A and B viruses form acid-activated proton channels that are essential for the virus lifecycle. Proton selectivity is achieved by a transmembrane (TM) histidine whereas gating is achieved by a tryptophan residue. Although this functional apparatus is conserved between AM2 and BM2 channels, AM2 conducts protons exclusively inward whereas BM2 conducts protons in either direction depending on the pH gradient. Previous studies showed that in AM2, mutations of D44 abolished inward rectification of AM2, suggesting that the tryptophan gate is destabilized. To elucidate how charged residues C-terminal to the tryptophan regulates channel gating, here we investigate the structure and dynamics of H19 and W23 in a BM2 mutant, GDR-BM2, in which three BM2 residues are mutated to the corresponding AM2 residues, S16G, G26D and H27R. Whole-cell electrophysiological data show that GDR-BM2 conducts protons with inward rectification, identical to wild-type (WT) AM2 but different from WT-BM2. Solid-state NMR

Indexed as

HistidineInfluenza B virusProtonsTryptophanViral Matrix ProteinsHydrogen-Ion ConcentrationInfluenza A virusIon ChannelsMolecular Dynamics SimulationMutationViroporin ProteinsHistidineIon ChannelsM2 protein, Influenza A virusProtonsTryptophanViral Matrix ProteinsViroporin Proteins

Identifiers

PMID39037444

DOI10.1039/d4cp01648c

PMCPMC11290064

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