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Fab-dimerized glycan-reactive antibodies are a structural category of natural antibodies.
Williams, Wilton B; Meyerhoff, R Ryan; Edwards, R J; Li, Hui; Manne, Kartik; Nicely, Nathan I; Henderson, Rory; Zhou, Ye; Janowska, Katarzyna; Mansouri, Katayoun; Gobeil, Sophie; Evangelous, Tyler; Hora, Bhavna; Berry, Madison; Abuahmad, A Yousef; Sprenz, Jordan; Deyton, Margaret; Stalls, Victoria; Kopp, Megan; Hsu, Allen L; Borgnia, Mario J; Stewart-Jones, Guillaume B E; Lee, Matthew S; Bronkema, Naomi; Moody, M Anthony; Wiehe, Kevin; Bradley, Todd; Alam, S Munir; Parks, Robert J; Foulger, Andrew; Oguin, Thomas; Sempowski, Gregory D; Bonsignori, Mattia; LaBranche, Celia C; Montefiori, David C; Seaman, Michael; Santra, Sampa; Perfect, John; Francica, Joseph R; Lynn, Geoffrey M; Aussedat, Baptiste; Walkowicz, William E; Laga, Richard; Kelsoe, Garnett; Saunders, Kevin O; Fera, Daniela; Kwong, Peter D; Seder, Robert A; Bartesaghi, Alberto; Shaw, George M.
  • Williams WB; Duke Human Vaccine Institute, Durham, NC 27710, USA; Department of Medicine, Duke University, Durham, NC 27710, USA. Electronic address: wilton.williams@duke.edu.
  • Meyerhoff RR; Duke Human Vaccine Institute, Durham, NC 27710, USA; Department of Medicine, Duke University, Durham, NC 27710, USA.
  • Edwards RJ; Duke Human Vaccine Institute, Durham, NC 27710, USA; Department of Medicine, Duke University, Durham, NC 27710, USA.
  • Li H; Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
  • Manne K; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Nicely NI; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Henderson R; Duke Human Vaccine Institute, Durham, NC 27710, USA; Department of Medicine, Duke University, Durham, NC 27710, USA.
  • Zhou Y; Department of Computer Science, Duke University, Durham, NC 27708, USA.
  • Janowska K; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Mansouri K; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Gobeil S; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Evangelous T; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Hora B; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Berry M; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Abuahmad AY; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Sprenz J; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Deyton M; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Stalls V; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Kopp M; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Hsu AL; Genome Integrity and Structural Biology Laboratory, NIEHS, NIH, Department of Health and Human Services, Research Triangle Park, NC 27709, USA.
  • Borgnia MJ; Genome Integrity and Structural Biology Laboratory, NIEHS, NIH, Department of Health and Human Services, Research Triangle Park, NC 27709, USA.
  • Stewart-Jones GBE; Vaccine Research Center, NIAID, NIH, Bethesda, MD 20892, USA.
  • Lee MS; Boston Children's Hospital and Harvard Medical School, Boston, MA 02115, USA.
  • Bronkema N; Department of Chemistry and Biochemistry, Swarthmore College, Swarthmore, PA 19081, USA.
  • Moody MA; Duke Human Vaccine Institute, Durham, NC 27710, USA; Department of Immunology, Duke University, Durham, NC 27710, USA; Department of Pediatrics, Duke University, Durham, NC 27710, USA.
  • Wiehe K; Duke Human Vaccine Institute, Durham, NC 27710, USA; Department of Medicine, Duke University, Durham, NC 27710, USA.
  • Bradley T; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Alam SM; Duke Human Vaccine Institute, Durham, NC 27710, USA; Department of Medicine, Duke University, Durham, NC 27710, USA.
  • Parks RJ; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Foulger A; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Oguin T; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Sempowski GD; Duke Human Vaccine Institute, Durham, NC 27710, USA; Department of Medicine, Duke University, Durham, NC 27710, USA.
  • Bonsignori M; Duke Human Vaccine Institute, Durham, NC 27710, USA; Department of Medicine, Duke University, Durham, NC 27710, USA.
  • LaBranche CC; Department of Surgery, Duke University, Durham, NC 27710, USA.
  • Montefiori DC; Duke Human Vaccine Institute, Durham, NC 27710, USA; Department of Surgery, Duke University, Durham, NC 27710, USA.
  • Seaman M; Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, MA 02215, USA.
  • Santra S; Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, MA 02215, USA.
  • Perfect J; Department of Medicine, Duke University, Durham, NC 27710, USA.
  • Francica JR; Vaccine Research Center, NIAID, NIH, Bethesda, MD 20892, USA.
  • Lynn GM; Vaccine Research Center, NIAID, NIH, Bethesda, MD 20892, USA; Avidea Technologies, Inc., Baltimore, MD, USA.
  • Aussedat B; Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
  • Walkowicz WE; Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
  • Laga R; Institute of Macromolecular Chemistry, Czech Academy of Sciences, Prague, Czech Republic.
  • Kelsoe G; Duke Human Vaccine Institute, Durham, NC 27710, USA; Department of Immunology, Duke University, Durham, NC 27710, USA.
  • Saunders KO; Duke Human Vaccine Institute, Durham, NC 27710, USA; Department of Immunology, Duke University, Durham, NC 27710, USA; Department of Surgery, Duke University, Durham, NC 27710, USA.
  • Fera D; Department of Chemistry and Biochemistry, Swarthmore College, Swarthmore, PA 19081, USA.
  • Kwong PD; Vaccine Research Center, NIAID, NIH, Bethesda, MD 20892, USA.
  • Seder RA; Vaccine Research Center, NIAID, NIH, Bethesda, MD 20892, USA.
  • Bartesaghi A; Department of Computer Science, Duke University, Durham, NC 27708, USA; Department of Biochemistry, Duke University, Durham, NC 27705, USA; Department of Electrical and Computer Engineering, Duke University, Durham, NC 27708, USA.
  • Shaw GM; Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
Cell ; 184(11): 2955-2972.e25, 2021 05 27.
Article in English | MEDLINE | ID: covidwho-1237636
Semantic information from SemMedBD (by NLM)
1. Antibodies INTERACTS_WITH Polysaccharides
Subject
Antibodies
Predicate
INTERACTS_WITH
Object
Polysaccharides
2. envelope PART_OF HIV-1
Subject
envelope
Predicate
PART_OF
Object
HIV-1
3. B-Lymphocytes PART_OF Macaca mulatta
Subject
B-Lymphocytes
Predicate
PART_OF
Object
Macaca mulatta
4. B-Lymphocytes PART_OF Homo sapiens
Subject
B-Lymphocytes
Predicate
PART_OF
Object
Homo sapiens
5. Cell surface LOCATION_OF Polysaccharides
Subject
Cell surface
Predicate
LOCATION_OF
Object
Polysaccharides
6. Pathogenic organism LOCATION_OF Polysaccharides
Subject
Pathogenic organism
Predicate
LOCATION_OF
Object
Polysaccharides
7. B-Lymphocytes PART_OF Marginal Zone
Subject
B-Lymphocytes
Predicate
PART_OF
Object
Marginal Zone
8. Antibodies INTERACTS_WITH Polysaccharides
Subject
Antibodies
Predicate
INTERACTS_WITH
Object
Polysaccharides
9. envelope PART_OF HIV-1
Subject
envelope
Predicate
PART_OF
Object
HIV-1
10. B-Lymphocytes PART_OF Macaca mulatta
Subject
B-Lymphocytes
Predicate
PART_OF
Object
Macaca mulatta
11. B-Lymphocytes PART_OF Homo sapiens
Subject
B-Lymphocytes
Predicate
PART_OF
Object
Homo sapiens
12. Cell surface LOCATION_OF Polysaccharides
Subject
Cell surface
Predicate
LOCATION_OF
Object
Polysaccharides
13. Pathogenic organism LOCATION_OF Polysaccharides
Subject
Pathogenic organism
Predicate
LOCATION_OF
Object
Polysaccharides
14. B-Lymphocytes PART_OF Marginal Zone
Subject
B-Lymphocytes
Predicate
PART_OF
Object
Marginal Zone
ABSTRACT
Natural antibodies (Abs) can target host glycans on the surface of pathogens. We studied the evolution of glycan-reactive B cells of rhesus macaques and humans using glycosylated HIV-1 envelope (Env) as a model antigen. 2G12 is a broadly neutralizing Ab (bnAb) that targets a conserved glycan patch on Env of geographically diverse HIV-1 strains using a unique heavy-chain (VH) domain-swapped architecture that results in fragment antigen-binding (Fab) dimerization. Here, we describe HIV-1 Env Fab-dimerized glycan (FDG)-reactive bnAbs without VH-swapped domains from simian-human immunodeficiency virus (SHIV)-infected macaques. FDG Abs also recognized cell-surface glycans on diverse pathogens, including yeast and severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike. FDG precursors were expanded by glycan-bearing immunogens in macaques and were abundant in HIV-1-naive humans. Moreover, FDG precursors were predominately mutated IgM+IgD+CD27+, thus suggesting that they originated from a pool of antigen-experienced IgM+ or marginal zone B cells.
Subject(s)
Keywords

Full text: Available Collection: International databases Database: MEDLINE Main subject: Polysaccharides / Immunoglobulin Fab Fragments / HIV-1 / Simian Immunodeficiency Virus / Env Gene Products, Human Immunodeficiency Virus / Antibodies, Neutralizing / Spike Glycoprotein, Coronavirus / SARS-CoV-2 Type of study: Randomized controlled trials Topics: Vaccines Limits: Animals / Humans Language: English Journal: Cell Year: 2021 Document Type: Article

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Polysaccharides / Immunoglobulin Fab Fragments / HIV-1 / Simian Immunodeficiency Virus / Env Gene Products, Human Immunodeficiency Virus / Antibodies, Neutralizing / Spike Glycoprotein, Coronavirus / SARS-CoV-2 Type of study: Randomized controlled trials Topics: Vaccines Limits: Animals / Humans Language: English Journal: Cell Year: 2021 Document Type: Article