Maria Carrasco-Rios

Utrecht, UT, Netherlands

Last Updated: 09/26/2026

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Found 10 publications

Acquisition of specific human respiratory tract binding by 2.3.4.4b H5N1 hemagglutinins requires multiple mutations.

Acquisition of specific human respiratory tract binding by 2.3.4.4b H5N1 hemagglutinins requires multiple mutations.

Journal: Journal of virology

Published: August 10, 2026

H5N1 2.3.4.4b HA E190D and Q226H mutations, picked up as minority variants in a patient, result in an inability to bind sialic acid.

H5N1 2.3.4.4b HA E190D and Q226H mutations, picked up as minority variants in a patient, result in an inability to bind sialic acid.

Journal: Virology

Published: March 13, 2026

The receptor binding properties of H5Ny influenza A viruses have evolved to bind to avian-type mucin-like O-glycans.

The receptor binding properties of H5Ny influenza A viruses have evolved to bind to avian-type mucin-like O-glycans.

Journal: PLoS pathogens

Published: June 03, 2025

The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors.

The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors.

Journal: Proceedings of the National Academy of Sciences of the United States of America

Published: April 15, 2025

The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors.

The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors.

Journal: bioRxiv : the preprint server for biology

Published: January 20, 2025

The mammary glands of cows abundantly display receptors for circulating avian H5 viruses.

The mammary glands of cows abundantly display receptors for circulating avian H5 viruses.

Journal: Journal of virology

Published: October 10, 2024

Complex N-glycans are important for interspecies transmission of H7 influenza A viruses.

Complex N-glycans are important for interspecies transmission of H7 influenza A viruses.

Journal: Journal of virology

Published: March 12, 2024

SARS-CoV-2 Spike N-Terminal Domain Engages 9-O-Acetylated α2-8-Linked Sialic Acids.

SARS-CoV-2 Spike N-Terminal Domain Engages 9-O-Acetylated α2-8-Linked Sialic Acids.

Journal: ACS chemical biology

Published: April 27, 2023

The SARS-CoV-2 spike N-terminal domain engages 9- O -acetylated α2-8-linked sialic acids.

The SARS-CoV-2 spike N-terminal domain engages 9- O -acetylated α2-8-linked sialic acids.

Journal: bioRxiv : the preprint server for biology

Published: October 20, 2022

N-Glycolylneuraminic Acid Binding of Avian and Equine H7 Influenza A Viruses.

N-Glycolylneuraminic Acid Binding of Avian and Equine H7 Influenza A Viruses.

Journal: Journal of virology

Published: January 19, 2022

Showing 1-10 of 10

Last Updated: 09/26/2026