Grilled Cheese

ExploreLog inSign up
Terms of UsePrivacy PolicyCommunity StandardsHelpGet the app

Grilled Cheese is a product of Village Compute

Version devBuilt at: 2026-10-10 01:38:52 EDT

Explore

PostsPeople
LatestRanked
@plosbiology.orgOct 1, 2026, 4:03 PM

Broadly neutralizing #flu #antibodies able to recognize both influenza A and B viruses are exceptionally rare. This study shows that mutations that promote binding to one flu virus can weaken recognition of others, constraining antibody cross-reactive breadth.
🧪 #ImmuneSky
plos.io/4z8mzGV

Structural analysis of the differential effects on binding affinity. (A) The Cαs of VH S24, VH S52, VH F54, and VH I73 in CR9114 are shown as spheres (PDB 4FQI) [15]. CR9114 and HA are in blue and white, respectively. The local chemical environment for (B) VH S24, (C) VH S52 and VH F54, and (D) VH I73 are shown. Black dashed lines represent H-bonds. (E) The structure of HA-bound CR9114 with VH W73 is modeled. Red circle indicates steric clash.
@plosbiology.orgSep 30, 2026, 12:01 PM

Broadly neutralizing #flu #antibodies able to recognize both influenza A and B viruses are exceptionally rare. This study shows that mutations that promote binding to one flu virus can weaken recognition of others, constraining antibody cross-reactive breadth.
🧪 #ImmuneSky
plos.io/4z8mzGV

Structural analysis of the differential effects on binding affinity. (A) The Cαs of VH S24, VH S52, VH F54, and VH I73 in CR9114 are shown as spheres (PDB 4FQI) [15]. CR9114 and HA are in blue and white, respectively. The local chemical environment for (B) VH S24, (C) VH S52 and VH F54, and (D) VH I73 are shown. Black dashed lines represent H-bonds. (E) The structure of HA-bound CR9114 with VH W73 is modeled. Red circle indicates steric clash.
@plosbiology.orgSep 29, 2026, 8:00 AM

Broadly neutralizing #flu #antibodies able to recognize both influenza A and B viruses are exceptionally rare. This study shows that mutations that promote binding to one flu virus can weaken recognition of others, constraining antibody cross-reactive breadth.
🧪 #ImmuneSky
plos.io/4z8mzGV

Structural analysis of the differential effects on binding affinity. (A) The Cαs of VH S24, VH S52, VH F54, and VH I73 in CR9114 are shown as spheres (PDB 4FQI) [15]. CR9114 and HA are in blue and white, respectively. The local chemical environment for (B) VH S24, (C) VH S52 and VH F54, and (D) VH I73 are shown. Black dashed lines represent H-bonds. (E) The structure of HA-bound CR9114 with VH W73 is modeled. Red circle indicates steric clash.
@plosbiology.orgSep 25, 2026, 4:10 PM

#PhageTherapy can fail when the immune system makes antibodies against therapeutic viruses. This study shows that fiber- and nozzle-specific antibodies block phage infection and promote aggregation-driven, Fc receptor-independent phagocytosis.
🧪 #ImmuneSky #structure #virus
buff.ly/J0FOg9g

The image shows a reconstructed model of antibody-induced phage aggregation. Phage therapy, which uses bacteria-specific viruses to treat bacterial infections, is a highly promising therapeutic strategy in the era of precision medicine. Increasing evidence suggests that antibodies generated during phage therapy can affect the efficacy of phage therapy and, in some cases, even lead to treatment failure. However, the molecular mechanisms by which phage-specific antibodies cause phage therapy failure remain to be elucidated. Using Acinetobacter baumannii and its podovirus phage AbP20 as a model, the authors revealed the antibodies targeting phage fiber and nozzle proteins induced the formation of large-sized tail-to-tail phage aggregates which possess reduced infection and facilitated susceptibility to phagocytosis, providing a new clue to understand phage-specific antibodies induced therapy failure. This image was created by Heng Xue and Hang Yang.
@plosbiology.orgSep 24, 2026, 12:10 PM

#PhageTherapy can fail when the immune system makes antibodies against therapeutic viruses. This study shows that fiber- and nozzle-specific antibodies block phage infection and promote aggregation-driven, Fc receptor-independent phagocytosis.
🧪 #ImmuneSky #structure #virus
buff.ly/J0FOg9g

The image shows a reconstructed model of antibody-induced phage aggregation. Phage therapy, which uses bacteria-specific viruses to treat bacterial infections, is a highly promising therapeutic strategy in the era of precision medicine. Increasing evidence suggests that antibodies generated during phage therapy can affect the efficacy of phage therapy and, in some cases, even lead to treatment failure. However, the molecular mechanisms by which phage-specific antibodies cause phage therapy failure remain to be elucidated. Using Acinetobacter baumannii and its podovirus phage AbP20 as a model, the authors revealed the antibodies targeting phage fiber and nozzle proteins induced the formation of large-sized tail-to-tail phage aggregates which possess reduced infection and facilitated susceptibility to phagocytosis, providing a new clue to understand phage-specific antibodies induced therapy failure. This image was created by Heng Xue and Hang Yang.
@plosbiology.orgSep 23, 2026, 8:10 AM

#PhageTherapy can fail when the immune system makes antibodies against therapeutic viruses. This study shows that fiber- and nozzle-specific antibodies block phage infection and promote aggregation-driven, Fc receptor-independent phagocytosis.
🧪 #ImmuneSky #structure #virus
buff.ly/J0FOg9g

The image shows a reconstructed model of antibody-induced phage aggregation. Phage therapy, which uses bacteria-specific viruses to treat bacterial infections, is a highly promising therapeutic strategy in the era of precision medicine. Increasing evidence suggests that antibodies generated during phage therapy can affect the efficacy of phage therapy and, in some cases, even lead to treatment failure. However, the molecular mechanisms by which phage-specific antibodies cause phage therapy failure remain to be elucidated. Using Acinetobacter baumannii and its podovirus phage AbP20 as a model, the authors revealed the antibodies targeting phage fiber and nozzle proteins induced the formation of large-sized tail-to-tail phage aggregates which possess reduced infection and facilitated susceptibility to phagocytosis, providing a new clue to understand phage-specific antibodies induced therapy failure. This image was created by Heng Xue and Hang Yang.