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TitleSimilarities and differences between native HIV-1 envelope glycoprotein trimers and stabilized soluble trimer mimetics.
Journal, issue, pagesPLoS Pathog, Vol. 15, Issue 7, Page e1007920, Year 2019
Publish dateJul 15, 2019
AuthorsAlba Torrents de la Peña / Kimmo Rantalainen / Christopher A Cottrell / Joel D Allen / Marit J van Gils / Jonathan L Torres / Max Crispin / Rogier W Sanders / Andrew B Ward /
PubMed AbstractThe HIV-1 envelope glycoprotein (Env) trimer is located on the surface of the virus and is the target of broadly neutralizing antibodies (bNAbs). Recombinant native-like soluble Env trimer mimetics, ...The HIV-1 envelope glycoprotein (Env) trimer is located on the surface of the virus and is the target of broadly neutralizing antibodies (bNAbs). Recombinant native-like soluble Env trimer mimetics, such as SOSIP trimers, have taken a central role in HIV-1 vaccine research aimed at inducing bNAbs. We therefore performed a direct and thorough comparison of a full-length unmodified Env trimer containing the transmembrane domain and the cytoplasmic tail, with the sequence matched soluble SOSIP trimer, both based on an early Env sequence (AMC011) from an HIV+ individual that developed bNAbs. The structures of the full-length AMC011 trimer bound to either bNAb PGT145 or PGT151 were very similar to the structures of SOSIP trimers. Antigenically, the full-length and SOSIP trimers were comparable, but in contrast to the full-length trimer, the SOSIP trimer did not bind at all to non-neutralizing antibodies, most likely as a consequence of the intrinsic stabilization of the SOSIP trimer. Furthermore, the glycan composition of full-length and SOSIP trimers was similar overall, but the SOSIP trimer possessed slightly less complex and less extensively processed glycans, which may relate to the intrinsic stabilization as well as the absence of the membrane tether. These data provide insights into how to best use and improve membrane-associated full-length and soluble SOSIP HIV-1 Env trimers as immunogens.
External linksPLoS Pathog / PubMed:31306470 / PubMed Central
MethodsEM (single particle)
Resolution4.2 - 28.0 Å
Structure data

EMDB-20106:
Full length HIV-1 Env AMC011 in complex with PGT151 Fab - DOPC bicelle
Method: EM (single particle) / Resolution: 28.0 Å

EMDB-20107:
Full length HIV-1 Env AMC011 in complex with PGT145 Fab - DOPC-CHS bicelle
Method: EM (single particle) / Resolution: 23.0 Å

EMDB-20108:
HIV-1 Env AMC011 SOSIP in complex with PGT145 Fab
Method: EM (single particle) / Resolution: 20.0 Å

20118

6olp

EMDB-20118, PDB-6olp:
Full length HIV-1 Env AMC011 in complex with PGT151 Fab
Method: EM (single particle) / Resolution: 4.2 Å

9378

6nij

EMDB-9378, PDB-6nij:
PGT145 Fab in complex with full length AMC011 HIV-1 Env
Method: EM (single particle) / Resolution: 5.7 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • human immunodeficiency virus 1
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / HIV-1 / antibody / glycoprotein / Viral Protein/IMMUNE SYSTEM / Viral Protein-IMMUNE SYSTEM complex

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