#epistasis — Public Fediverse posts

Structural and molecular #basis of the #epistasis effect in enhanced affinity between #SARS-CoV-2 #KP3 and #ACE2 http://biorxiv.org/cgi/content/short/2024.09.03.610799v1?rss=1

KP.3, featuring F456L and Q493E, exhibits a markedly enhanced ACE2 binding affinity compared to #KP2 and #JN1 #variant due to synergistic effects between these mutations.

Structural and molecular #basis of the #epistasis effect in enhanced affinity between #SARS-CoV-2 #KP3 and #ACE2 http://biorxiv.org/cgi/content/short/2024.09.03.610799v1?rss=1

KP.3, featuring F456L and Q493E, exhibits a markedly enhanced ACE2 binding affinity compared to #KP2 and #JN1 #variant due to synergistic effects between these mutations.

Structural and molecular #basis of the #epistasis effect in enhanced affinity between #SARS-CoV-2 #KP3 and #ACE2 http://biorxiv.org/cgi/content/short/2024.09.03.610799v1?rss=1

KP.3, featuring F456L and Q493E, exhibits a markedly enhanced ACE2 binding affinity compared to #KP2 and #JN1 #variant due to synergistic effects between these mutations.

Structural and molecular #basis of the #epistasis effect in enhanced affinity between #SARS-CoV-2 #KP3 and #ACE2 http://biorxiv.org/cgi/content/short/2024.09.03.610799v1?rss=1

KP.3, featuring F456L and Q493E, exhibits a markedly enhanced ACE2 binding affinity compared to #KP2 and #JN1 #variant due to synergistic effects between these mutations.

Structural and molecular #basis of the #epistasis effect in enhanced affinity between #SARS-CoV-2 #KP3 and #ACE2 http://biorxiv.org/cgi/content/short/2024.09.03.610799v1?rss=1

KP.3, featuring F456L and Q493E, exhibits a markedly enhanced ACE2 binding affinity compared to #KP2 and #JN1 #variant due to synergistic effects between these mutations.

#Epistasis mediates the evolution of #receptor binding mode in recent #human #H3N2 #hemagglutinin, Nat Commun.: https://www.nature.com/articles/s41467-024-49487-4

Combinatorial #mutagenesis reveals that G186D and D190N, along with other natural mutations in recent H3N2 strains, alter compatibility with a common egg-adaptive mutation in seasonal influenza vaccines. Our findings elucidate role of epistasis in shaping recent evolution of human hemagglutinin & substantiate high evolvability of its receptor-binding mode.

#Epistasis mediates the evolution of #receptor binding mode in recent #human #H3N2 #hemagglutinin, Nat Commun.: https://www.nature.com/articles/s41467-024-49487-4

Combinatorial #mutagenesis reveals that G186D and D190N, along with other natural mutations in recent H3N2 strains, alter compatibility with a common egg-adaptive mutation in seasonal influenza vaccines. Our findings elucidate role of epistasis in shaping recent evolution of human hemagglutinin & substantiate high evolvability of its receptor-binding mode.

New paper with @CCWendling Co-transfer of functionally interdependent genes contributes to genome mosaicism in lambdoid phages - we use an approach that does not rely on the core genome phylogeny to infer gene transfers, and then detect co-transferred genes in lambdoid phages, we highlight known and novel co-transfer examples

#phage #evolution #recombination #HGT #Epistasis
https://www.microbiologyresearch.org/content/journal/mgen/10.1099/mgen.0.000915

#introduction I mostly work using in silico experiments and mathematical modeling to understand how properties of biological systems affect their evolution. Some of the topics I have studied include:

The effect of #epistasis in the accumulation and purging of deleterious mutations in organisms with high mutation rates. #mutationload

How the #modularity of
#DevelopmentalProcesses affect the #PhenotypicVariability of biological systems. #IntroductionBias