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| Title | Antibodies from primary humoral responses modulate the recruitment of naive B cells during secondary responses. |
|---|---|
| Journal, issue, pages | Immunity, Vol. 55, Issue 10, Page 1856-11871.e6, Year 2022 |
| Publish date | Oct 11, 2022 |
 Authors | Jeroen M J Tas / Ja-Hyun Koo / Ying-Cing Lin / Zhenfei Xie / Jon M Steichen / Abigail M Jackson / Blake M Hauser / Xuesong Wang / Christopher A Cottrell / Jonathan L Torres / John E Warner / Kathrin H Kirsch / Stephanie R Weldon / Bettina Groschel / Bartek Nogal / Gabriel Ozorowski / Sandhya Bangaru / Nicole Phelps / Yumiko Adachi / Saman Eskandarzadeh / Michael Kubitz / Dennis R Burton / Daniel Lingwood / Aaron G Schmidt / Usha Nair / Andrew B Ward / William R Schief / Facundo D Batista /  |
| PubMed Abstract | Vaccines generate high-affinity antibodies by recruiting antigen-specific B cells to germinal centers (GCs), but the mechanisms governing the recruitment to GCs on secondary challenges remain unclear. ...Vaccines generate high-affinity antibodies by recruiting antigen-specific B cells to germinal centers (GCs), but the mechanisms governing the recruitment to GCs on secondary challenges remain unclear. Here, using preclinical SARS-CoV and HIV mouse models, we demonstrated that the antibodies elicited during primary humoral responses shaped the naive B cell recruitment to GCs during secondary exposures. The antibodies from primary responses could either enhance or, conversely, restrict the GC participation of naive B cells: broad-binding, low-affinity, and low-titer antibodies enhanced recruitment, whereas, by contrast, the high titers of high-affinity, mono-epitope-specific antibodies attenuated cognate naive B cell recruitment. Thus, the directionality and intensity of that effect was determined by antibody concentration, affinity, and epitope specificity. Circulating antibodies can, therefore, be important determinants of antigen immunogenicity. Future vaccines may need to overcome-or could, alternatively, leverage-the effects of circulating primary antibodies on subsequent naive B cell recruitment. |
 External links | Immunity / PubMed:35987201 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 19.0 - 25.0 Å |
| Structure data |  EMDB-27036: N332-GT2 trimer in complex with pooled polyclonal fab from BG18-exposed mice (day 14)  EMDB-27037: N332-GT2 trimer in complex with pooled polyclonal fab from wild type mice (day 42)  EMDB-27038: N332-GT2 trimer in complex with pooled polyclonal fab from BG18-exposed mice (day 42)  EMDB-27039: SARS-CoV-2 S protein mix in complex with Novavax NHP 36057 polyclonal Fab  EMDB-27040: SARS-CoV-2 S protein mix in complex with Novavax NHP 36964 polyclonal Fab  EMDB-27041: SARS-CoV-2 S protein mix in complex with Novavax NHP 37452 polyclonal Fab  EMDB-27042: SARS-CoV-2 S protein mix in complex with Novavax NHP 37611 polyclonal Fab  EMDB-27197: SARS-CoV-2 spike protein complexed with polyclonal Fab from donor D (Donor Lotus-25)  EMDB-27198: SARS-CoV-2 spike protein complexed with polyclonal Fab from donor C (Donor 1992)  EMDB-27199: SARS-CoV-2 spike protein complexed with polyclonal Fab from donor B (Donor 1989)  EMDB-27200: SARS-CoV-2 spike protein complexed with polyclonal Fab from donor A (Donor 1988) |
| Source |
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Human immunodeficiency virus
