[ { "id": "https://authors.library.caltech.edu/records/411nh-04f54", "eprint_id": 112445, "eprint_status": "archive", "datestamp": "2023-08-20 04:32:58", "lastmod": "2023-12-22 23:31:18", "type": "conference_item", "metadata_visibility": "show", "creators": { "items": [ { "id": "Bjorkman-P-J", "name": { "family": "Bjorkman", "given": "Pamela J." }, "orcid": "0000-0002-2277-3990" } ] }, "title": "Neutralizing antibodies against coronaviruses", "ispublished": "unpub", "full_text_status": "restricted", "note": "\u00a9 2021 American Chemical Society.", "abstract": "The SARS-CoV-2 virus has caused a world-wide pandemic resulting in a massive loss of lives and detrimental effects on the economies of most countries. We are using single-particle cryo-electron microscopy (cryo-EM) to solve structures of infection- and vaccination-induced antibodies complexed with the spike trimer of SARS-CoV-2 in order to elucidate the structural correlates of antibody-based immune protection. Structural comparisons allowed us to classify antibodies against the receptor-binding domain (RBD) of spike trimer into categories. These classifications and structural analyses provide rules for assigning current and future human RBD-targeting antibodies into classes, evaluating avidity effects, and suggesting combinations for clin. use, and provide insight into immune responses against SARS-CoV-2. Our structural studies have also guided the development of a potential pan-betacoronavirus vaccine. The vaccine approach involves co-display of diverse sets of RBDs from SARS-like beta coronaviruses (sarbecoviruses) on nanoparticles (mosaic-RBD-nanoparticles) that results in increased breadth of neutralizing responses in mice compared with nanoparticles presenting only SARS-CoV-2 RBDs. This modular vaccine platform could provide protection from SARS-CoV-2 as well as potential future emergent coronaviruses that could cause pandemics.", "date": "2021-08", "date_type": "published", "publisher": "Caltech Library", "id_number": "CaltechAUTHORS:20211214-231246715", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20211214-231246715", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "local_group": { "items": [ { "id": "COVID-19" }, { "id": "Division-of-Biology-and-Biological-Engineering" } ] }, "resource_type": "conference_item", "pub_year": "2021", "author_list": "Bjorkman, Pamela J." }, { "id": "https://authors.library.caltech.edu/records/80vxb-zz649", "eprint_id": 57200, "eprint_status": "archive", "datestamp": "2023-08-20 03:51:28", "lastmod": "2023-10-23 17:09:12", "type": "conference_item", "metadata_visibility": "show", "creators": { "items": [ { "id": "Ndjamen-B", "name": { "family": "Ndjamen", "given": "B." } }, { "id": "Fraser-S-E", "name": { "family": "Fraser", "given": "S. E." }, "orcid": "0000-0002-5377-0223" }, { "id": "Bjorkman-P-J", "name": { "family": "Bjorkman", "given": "P. J." }, "orcid": "0000-0002-2277-3990" } ] }, "title": "Distinct Intracellular Trafficking Patterns of Host IgG by Herpes Virus Fc-Receptors", "ispublished": "unpub", "full_text_status": "public", "note": "\u00a9 American Society for Cell Biology. POSTER PRESENTATIONS- Sunday, December 7.\n\n
Published - Ndjamen_2014pP1217.pdf
", "abstract": "Members of both alpha and beta herpes viruses affects 50\u201398% of people around the world. They cause severe symptoms in congenitally infected newborns, a lifelong latent infection that is lethal in immunocompromised\nindividuals, and are associated with several types of cancer. Human cytomegalovirus (HCMV) and herpes simplex virus type 1 (HSV-1) viruses express proteins (HCMV gp68 and gp34; HSV-1 gE-gI) that function as Fc receptors (FcRs) by binding to the Fc regions of human IgG. In addition to\nbinding free IgG, these viral FcRs can bind to IgG complexed with an antigen to form an antibody bipolar\nbridged (ABB) complex. Although HCMV gp68 and HSV-1 gE-gI have an overlapping binding site on Fc, the finding that the gp68/Fc interaction is stable at pH values between 5.6 and 8.1 but that gE-gI binds only at neutral or basic pH suggests distinct pH-based downstream events after IgG is internalized via receptor-mediated endocytosis into intracellular compartments. Here we developed a cell-based in vitro model system to define the fates of ABB complexes formed by the two types of viral FcRs. We found that alpha (HSV-1) and beta (HCMV) herpes virus FcRs displayed distinct intracellular trafficking patterns to target internalized ligands: HSV-1 gE-gI dissociates from its IgG-antigen ligand in acidic endosomal compartments and recycles back to the cell surface, whereas HCMV FcRs (gp68) are transported together with IgG-antigen complexes to lysosomes for degradation. In both cases, anti-viral IgGs and their viral targets are selectively degraded, a potential immune evasion strategy allowing herpes viruses\nto escape from IgG-mediated immune responses.", "date": "2014-12", "date_type": "published", "publisher": "Caltech Library", "id_number": "CaltechAUTHORS:20150504-125103596", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20150504-125103596", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "contributors": { "items": [ { "id": "Lippincott-Schwartz -J", "name": { "family": "Lippincott-Schwartz", "given": "Jennifer" } }, { "id": "Marshall-W", "name": { "family": "Marshall", "given": "Wallace" } }, { "id": "Marks-M", "name": { "family": "Marks", "given": "Michael" } } ] }, "primary_object": { "basename": "Ndjamen_2014pP1217.pdf", "url": "https://authors.library.caltech.edu/records/80vxb-zz649/files/Ndjamen_2014pP1217.pdf" }, "resource_type": "conference_item", "pub_year": "2014", "author_list": "Ndjamen, B.; Fraser, S. E.; et el." } ]