Potent Neutralization by Antibodies Targeting the Mpox A28 Protein
Yefet, R.; Battini, L.; Hubert, M.; Rakayev, K.; GUIVEL-BENHASSINE, F.; Rattner, N.; Porrot, F.; Abramovitz, L.; Ostashinsky, G.; Ben-Shalom, N.; Postal, J.; Polonsky, K.; Ralph-Altman, M.; Sweed, S.; Korner, T.; Friedel, N.; Hagin, D.; Sprecher, E.; Fishelson, Z.; Kobiler, O.; Adler-Abramovich, L.; Schwartz, O.; Guardado-Calvo, P.; Freund, N.
Show abstract
Mpox is the most pathogenic Poxvirus in circulation. While several antigens have been identified as targets for neutralizing antibodies, many proteins remain unexplored. We isolated and characterized four monoclonal antibodies (mAbs) targeting the Mpox A28 (OPG153), a virulence factor present on mature Mpox virions. The antibodies were isolated from convalescent individuals, alongside 14 additional mAbs targeting the A35 and H3 proteins. Anti-A28 mAbs potently neutralized Mpox and Vaccinia virus (VACV) through complement-dependent mechanisms involving C1q and C3 deposition. High resolution crystal structures of Anti-A28 mAbs 10M2146 and 8M2110 in complex with VACV A26 revealed two proximal epitopes within the N-terminal domain. Passive transfer of 8M2110 attenuated disease in infected mice. Moreover, immunization with A28 elicited antigen-specific B cells and robust neutralizing antibody responses and provided complete protection against lethal VACV challenge. These findings support Mpox A28 as a promising target for the induction of neutralizing antibodies and antiviral interventions.
Matching journals
The top 6 journals account for 50% of the predicted probability mass.
Similar papers in this journal
Similar papers in this journal
Similar papers in this journal
- Replication-dead gammaherpesvirus vaccine protects against acute replication, reactivation from latency, and lethal challenge in mice 97%
- Antibody elicited by HIV-1 immunogen vaccination in macaques displaces Env fusion peptide and destroys a neutralizing epitope 97%
- Immunofocusing on the conserved fusion peptide of HIV envelope glycoprotein in rhesus macaques 97%
Similar papers in this journal
- A monoclonal antibody targeting the Nipah virus fusion glycoprotein apex imparts protection from disease 98%
- Design of SARS-CoV-2 RBD Immunogens to Focus Immune Responses Towards Conserved Coronavirus Epitopes 98%
- A human cytomegalovirus prefusion-like glycoprotein B subunit vaccine elicits similar humoral immunity to that of postfusion gB in mice 97%
Similar papers in this journal
- A protective and broadly binding antibody class engages the influenza virus hemagglutinin head at its stem interface 98%
- Surface-modified measles vaccines encoding oligomeric, fusion-stabilized SARS-CoV-2 spike glycoproteins bypass measles seropositivity, boosting neutralizing antibody responses to omicron and historical variants. 97%
- Acute malaria dysregulates specialized lymph node macrophages to suppress vaccine-elicited protection against Ebola virus 97%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.