Lassa Fever Virus Binds Matriglycan-A Polymer of Alternating Xylose and Glucuronate-On α-Dystroglycan.


Journal

Viruses
ISSN: 1999-4915
Titre abrégé: Viruses
Pays: Switzerland
ID NLM: 101509722

Informations de publication

Date de publication:
25 08 2021
Historique:
received: 21 07 2021
revised: 18 08 2021
accepted: 20 08 2021
entrez: 28 9 2021
pubmed: 29 9 2021
medline: 10 2 2022
Statut: epublish

Résumé

Lassa fever virus (LASV) can cause life-threatening hemorrhagic fevers for which there are currently no vaccines or targeted treatments. The late Prof. Stefan Kunz, along with others, showed that the high-affinity host receptor for LASV, and other Old World and clade-C New World mammarenaviruses, is matriglycan-a linear repeating disaccharide of alternating xylose and glucuronic acid that is polymerized uniquely on α-dystroglycan by like-acetylglucosaminyltransferase-1 (LARGE1). Although α-dystroglycan is ubiquitously expressed, LASV preferentially infects vascular endothelia and professional phagocytic cells, which suggests that viral entry requires additional cell-specific factors. In this review, we highlight the work of Stefan Kunz detailing the molecular mechanism of LASV binding and discuss the requirements of receptors, such as tyrosine kinases, for internalization through apoptotic mimicry.

Identifiants

pubmed: 34578260
pii: v13091679
doi: 10.3390/v13091679
pmc: PMC8473316
pii:
doi:

Substances chimiques

Polymers 0
Receptors, Virus 0
Dystroglycans 146888-27-9
Glucuronic Acid 8A5D83Q4RW
Xylose A1TA934AKO

Types de publication

Journal Article Research Support, N.I.H., Extramural Review

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NINDS NIH HHS
ID : P50 NS053672
Pays : United States
Organisme : Paul D. Wellstone Muscular Dystrophy Specialized Research Center grant
ID : 1U54NS053672

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Auteurs

Soumya Joseph (S)

Howard Hughes Medical Institute, Senator Paul D. Wellstone Muscular Dystrophy Specialized Research Center, Department of Molecular Physiology and Biophysics and Department of Neurology, Roy J. and Lucille A. Carver College of Medicine, The University of Iowa, Iowa City, IA 52242, USA.

Kevin P Campbell (KP)

Howard Hughes Medical Institute, Senator Paul D. Wellstone Muscular Dystrophy Specialized Research Center, Department of Molecular Physiology and Biophysics and Department of Neurology, Roy J. and Lucille A. Carver College of Medicine, The University of Iowa, Iowa City, IA 52242, USA.

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Classifications MeSH