#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, https://etidiohnew.blogspot.com/2026/03/h5n1-2344b-ha-e190d-and-q226h-mutations.html
#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.

#Sialic acids are a #barrier to the entry of non-influenza #orthomyxoviruses

#Sialic Acid #Receptors in #Human Mammary Tissue: Implications for #Infection with Novel #Influenza Strains

#Avian and #Human #Influenza A Virus #Receptors in #Bovine #Mammary #Gland, Emerg Infect Dis.: https://wwwnc.cdc.gov/eid/article/30/9/24-0696_article

An outbreak of influenza A (#H5N1) virus was detected in dairy cows in the #USA. We detected influenza A virus #sialic acid -α2,3/α2,6-galactose host receptors in bovine mammary glands by lectin histochemistry. Our results provide a rationale for the high levels of H5N1 virus in #milk from infected cows.

Avian and Human Influenza A Virus Receptors in Bovine Mammary Gland

Influenza Virus Receptors in Bovine Mammary Gland

Emerging Infectious Diseases journal

#Bovine #H5N1 #influenza virus binds poorly to #human-type #sialic acid #receptors, BioRxIV: https://www.biorxiv.org/content/10.1101/2024.08.01.606177v1

Using two different methods, we found that both of the 2.3.4.4b H5s bound efficiently to glycan receptors with terminally linked a2-3 sialic acid with no detectable binding to glycan receptors with terminally linked a2-6 sialic acid.

#Cell #binding, uptake and #infection of #influenza A virus using recombinant #antibody-based #receptors. http://biorxiv.org/cgi/content/short/2024.07.29.605726v1?rss=1

#Human and #avian influenza A viruses bind to #sialic acid (Sia) receptors on cells as their primary receptors, and this results in endocytic uptake of the virus.

#H19 #influenza A virus exhibits #species-specific #MHC class II #receptor usage, Cell Host Microbe: https://www.cell.com/cell-host-microbe/abstract/S1931-3128(24)00190-2?rss=yes

Influenza A virus H19 subtype does not bind the canonical receptor #sialic acid. H19 utilizes MHC class II #proteins from distinct species for host cell entry.
Mutating the putative canonical RBS of H19 restores sialic acid dependency. Residues in the MHC class II α chain confer species-specific entry of H19.

#Expert #reaction #study on features of #infection & #transmission of #bovine #H5N1 #influenza, Science Media Centre: https://www.sciencemediacentre.org/expert-reaction-study-on-features-of-infection-and-transmission-of-bovine-h5n1-influenza/

“There are some novel characteristics of this work compared with other studies, such as demonstrating ability of the virus to bind to both a2, 3 & a2,6 #sialic acid. This is of concern as it suggests a possible increase in potential of this virus to infect other mammals, including humans...

expert reaction study on features of infection and transmission of bovine H5N1 influenza | Science Media Centre

#Pathogenicity and #transmissibility of #bovine #H5N1 #influenza virus, Nature: https://www.nature.com/articles/s41586-024-07766-6

Importantly, bovine HPAI H5N1 virus bound to #sialic acids expressed in #human upper #airways and inefficiently transmitted to exposed ferrets (one of four exposed ferrets seroconverted without virus detection). Bovine HPAI H5N1 virus thus possesses features that may facilitate #infection and #transmission in #mammals.

Pathogenicity and transmissibility of bovine H5N1 influenza virus - Nature

HPAI H5N1 virus isolated from infected cow milk is characterized in mice and ferrets, was inefficiently transmitted in ferrets, and bound to sialic acids expressed in human upper airways, showing features that may facilitate infection in mammals.

Nature