M. J. van Gils

This study identifies broadly neutralizing monoclonal and bispecific antibodies from a Gamma variant-infected individual that effectively neutralize multiple SARS-CoV-2 variants.

This study shows that antibodies against SARS-CoV-2 reduce complement-induced inflammation, suggesting a role for complement in immune activation and antibody-mediated immune regulation.

The paper identifies SYK and PI3K inhibitors, particularly entospletinib, as effective in counteracting anti-spike IgG-induced hyperinflammation in severe COVID-19.

This study shows bispecific antibodies combine the neutralizing breadth and potency of parental antibodies to neutralize SARS-CoV and SARS-CoV-2 variants, including Omicron.

The paper identifies a novel S2 epitope recognized by a public antibody class in SARS-CoV-2-reactive B cells, which becomes exposed on vaccine-optimized spike proteins.

This study shows SARS-CoV-2 does not activate dendritic cells via extracellular TLRs but instead relies on intracellular sensors after infecting ACE2-expressing dendritic cells.

The paper examines how mutations at E484 and K417 in SARS-CoV-2 variants affect neutralizing antibodies, showing reduced efficacy against certain antibody families but not others.

This study shows that combining cross-neutralizing antibodies CV38-142 and COVA1-16 enhances neutralization of SARS-CoV-2 and SARS-CoV pseudoviruses.

This study evaluates how Spike mutations in SARS-CoV-2 variants affect neutralization by monoclonal and polyclonal antibodies, showing reduced activity in some cases.

This study identifies heparan sulfate proteoglycans as SARS-CoV-2 attachment receptors and shows that LMWH blocks infection and transmission.

The paper identifies a SARS-CoV-2 antibody that cross-neutralizes SARS-CoV by binding a conserved epitope and relies on avidity for neutralization.

This study identifies an alternative binding mode of IGHV3-53 antibodies to the SARS-CoV-2 RBD, showing that longer CDR H3 can bind with different angles and interactions.

The paper modifies HIV-1 Env trimers to increase glycan occupancy and reduce artificial glycan holes, improving vaccine antigen design.

The paper shows that afucosylated IgG responses are common in enveloped virus infections and are more severe in COVID-19, with implications for immune response and pathology.

The paper investigates how HIV-1 envelope glycan networks affect the formation and stability of broadly neutralizing antibody epitopes, showing their importance in immunogen design.

This study maps antibody responses to HIV-1 envelope trimers in non-human primates, identifying strain-specific and conserved epitopes recognized by vaccine-induced antibodies.

The paper identifies monoclonal antibodies from rabbits that bind an epitope overlapping the N332 glycan supersite but not the glycan hole, suggesting strain-specific responses may interfere with broadly neutralizing antibodies.

This study shows that immunization with B41 and BG505 SOSIP trimer immunogens in rabbits induces distinct autologous neutralizing antibody lineages targeting overlapping glycan hole epitopes, but broadening reactivity remains challenging.

This study compares native HIV-1 Env trimers with soluble SOSIP trimers, finding structural and antigenic similarities but differences in antibody binding and glycan composition.