Breaking the Convention: Sialoglycan Variants, Coreceptors, and Alternative Receptors for Influenza A Virus Entry

Autor: Marie O. Pohl, Silke Stertz, Umut Karakus
Přispěvatelé: University of Zurich, Stertz, Silke
Rok vydání: 2020
Předmět:
10028 Institute of Medical Virology
1109 Insect Science
media_common.quotation_subject
Immunology
Neuraminidase
Virus Attachment
Hemagglutinin (influenza)
Hemagglutinin Glycoproteins
Influenza Virus

610 Medicine & health
Sialic acid binding
Biology
medicine.disease_cause
Major histocompatibility complex
Microbiology
03 medical and health sciences
chemistry.chemical_compound
0302 clinical medicine
Viral entry
Chiroptera
Virology
Influenza A virus
medicine
Animals
Humans
Receptor
Internalization
030304 developmental biology
media_common
2403 Immunology
0303 health sciences
Gem
2404 Microbiology
Histocompatibility Antigens Class II
Virus Internalization
N-Acetylneuraminic Acid
Sialic acid
HEK293 Cells
chemistry
Insect Science
2406 Virology
biology.protein
Receptors
Virus

570 Life sciences
biology
030217 neurology & neurosurgery
Zdroj: J Virol
ISSN: 1098-5514
0022-538X
Popis: The influenza A virus (IAV) envelope protein hemagglutinin binds α2,6- or α2,3-linked sialic acid as a host cell receptor. Bat IAV subtypes H17N10 and H18N11 form an exception to this rule and do not bind sialic acid but enter cells via major histocompatibility complex (MHC) class II. Here, we review current knowledge on IAV receptors with a focus on sialoglycan variants, protein coreceptors, and alternative receptors that impact IAV attachment and internalization beyond the well-described sialic acid binding.
Databáze: OpenAIRE