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#receptor

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Dual #receptor-binding, #infectivity, and #transmissibility of an emerging #H2N2 low pathogenicity avian #influenza virus

Source: Nature Communications, AbstractThe 1957 H2N2 influenza pandemic virus has disappeared from humans since 1968, while H2N2 avian influenza viruses (AIVs) are still circulating in birds. It is necessary to reveal the recurrence risk and potential cross-species infection of these AIVs from avian to mammals. We find that H2 AIVs circulating in…

etidioh.wordpress.com/2024/11/

ETIDIoH · Dual #receptor-binding, #infectivity, and #transmissibility of an emerging #H2N2 low pathogenicity avian #influenza virus
More from ETIDIoH

Structural basis for #receptor-binding domain mobility of the #spike in #SARS-CoV-2 #BA286 and #JN1

Source: Nature Communications, AbstractSince 2019, SARS-CoV-2 has undergone mutations, resulting in pandemic and epidemic waves. The SARS-CoV-2 spike protein, crucial for cellular entry, binds to the ACE2 receptor exclusively when its receptor-binding domain (RBD) adopts the up-conformation. However, whether ACE2 also interacts with the RBD in the down-conformation to…

etidioh.wordpress.com/2024/10/

ETIDIoH · Structural basis for #receptor-binding domain mobility of the #spike in #SARS-CoV-2 #BA286 and #JN1Source: Nature Communications, AbstractSince 2019, SARS-CoV-2 has undergone mutations, resulting in pandemic and epidemic waves. The SARS-CoV-2 spike protein, crucial for cellular entry, binds to t…

Theoretical #Investigations of a point #mutation affecting #H5 #HA’s #receptor binding preference, Comput Biol Chem.: sciencedirect.com/science/arti

#D94N #mutation on HA causes a shift in receptor binding preference from #avian-type SAα2,3Gal to #human-type SAα2,6Gal. Mutation causes an enhanced flexibility of the 130-Loop, leading to instability of HA-SAα2,3Gal complex. Resilience of interactions between HA & SAα2,6Gal is attributed to the inherent flexibility of glycan.

www.sciencedirect.comTheoretical Investigations of a point mutation affecting H5 Hemagglutinin’s receptor binding preferenceThe avian influenza A H5N1 virus is a subtype of influenza A virus (IAV) that causes a highly infectious and severe respiratory illness in birds and p…

#Structure defining of ultrapotent neutralizing #nanobodies against #MERS-CoV with novel epitopes on #receptor binding domain journals.plos.org/plospathogen

These results not only character unprecedented epitopes for antibody recognition but also provide promising agents for prophylaxis and therapy of MERS-CoV infection.

journals.plos.orgStructure defining of ultrapotent neutralizing nanobodies against MERS-CoV with novel epitopes on receptor binding domainAuthor summary MERS-CoV is one of the most prevalent zoonotic virus that has spread through 27 countries and infected more than 2,605 people since its first outbreak in Saudi Arabia in 2012. The high fatality rate and its persistent wide spread infectiousness in animal reservoirs have generated tremendous global public health concern. However, no licensed therapeutic agents or vaccines against MERS-CoV are currently available. To address the risk of MERS-CoV and its variants re-emergence, we developed four highly effective Nbs from alpaca and solved two crystal complexes of Nb9 and Nb14 with RBD. Remarkably, the neutralizing activity of Nb14 represents the highest of MERS-CoV antibodies reported to date. The novel epitopes of Nb14 and Nb9 locate outside the RBD and hDPP4 interface, and the unique different epitopes and mechanisms of Nb14 and Nb9 provide a better neutralizing for synergistically against MERS-CoV infection. Our findings provide insights into the cryptic epitopes on RBD and the development of antibodies against MERS-CoV infection.