Abstract:
:Oligomannose-type glycans on HIV-1 gp120 form a patch that is targeted by several broadly neutralizing antibodies (bnAbs) and that therefore is of interest to vaccine design. However, attempts to elicit similar oligomannose-specific bnAbs by immunizing with oligomannosidic glycoconjugates have only been modestly successful so far. A common assumption is that eliciting oligomannose-specific bnAbs is hindered by B cell tolerance, resulting from the presented oligomannosides being sensed as self molecules. Here, we present data, along with existing scientific evidence, supporting an additional, or perhaps alternate, explanation: serum mannosidase trimming of the presented oligomannosides in vivo. Mannosidase trimming lessens the likelihood of eliciting antibodies with capacity to bind full-sized oligomannose, which typifies the binding mode of existing bnAbs to the oligomannose patch. The rapidity of the observed trimming suggests the need for immunization strategies and/or synthetic glycosides that readily avoid or resist mannosidase trimming upon immunization and can overcome possible tolerance restrictions.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Bruxelle JF,Kirilenko T,Qureshi Q,Lu N,Trattnig N,Kosma P,Pantophlet Rdoi
10.1038/s41598-020-64500-8subject
Has Abstractpub_date
2020-05-05 00:00:00pages
7582issue
1issn
2045-2322pii
10.1038/s41598-020-64500-8journal_volume
10pub_type
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