Publications by authors named "Brent Oosthuysen"

Broadly neutralizing antibodies (bNAbs) that target the membrane-proximal external region (MPER) of HIV gp41 envelope, such as 4E10, VRC42.01 and PGZL1, can neutralize >80% of viruses. These three MPER-directed monoclonal antibodies share germline antibody genes (IGHV1-69 and IGKV3-20) and form a bNAb epitope class.

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The Janssen (Johnson & Johnson) Ad26.COV2.S non-replicating viral vector vaccine has been widely deployed for COVID-19 vaccination programs in resource-limited settings.

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The SARS-CoV-2 Omicron variant escapes neutralizing antibodies elicited by vaccines or infection. However, whether Omicron triggers cross-reactive humoral responses to other variants of concern (VOCs) remains unknown. We used plasma from 20 unvaccinated and 7 vaccinated individuals infected by Omicron BA.

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The ability of several broadly neutralizing antibodies (bNAbs) to protect against HIV infection is enhanced through Fc receptor binding. Antibody isotype modulates this effect, with IgG3 associated with improved HIV control and vaccine efficacy. We recently showed that an IgG3 variant of bNAb CAP256-VRC26.

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Article Synopsis
  • Neutralizing antibodies (nAbs) diversify during infection due to an "arms race" with viruses, where somatic hypermutation (SHM) helps antibodies adapt to new viral escape variants.
  • The study focuses on an HIV-directed nAb lineage, CAP88-CH06, revealing multiple co-circulating isotypes (IgG3, IgG1, IgA1, IgG2, IgA2) that can recognize similar viral targets.
  • It finds that IgG3 and IgA1 are more effective at neutralizing HIV variants compared to IgG1, and highlights a concept called "switch redemption," where detrimental class-switch recombination (CSR) events can be improved through further CSR, enhancing overall
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The human retinoblastoma binding protein 6 (RBBP6) is implicated in esophageal, lung, hepatocellular and colon cancers. Furthermore, RBBP6 was identified as a strong marker for colon cancer prognosis and as a predisposing factor in familial myeloproliferative neoplasms. Functionally, the mammalian protein interacts with p53 and enhances the activity of Mdm2, the prototypical negative regulator of p53.

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