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TitleDesign and structure of two HIV-1 clade C SOSIP.664 trimers that increase the arsenal of native-like Env immunogens.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 112, Issue 38, Page 11947-11952, Year 2015
Publish dateSep 22, 2015
AuthorsJean-Philippe Julien / Jeong Hyun Lee / Gabriel Ozorowski / Yuanzi Hua / Alba Torrents de la Peña / Steven W de Taeye / Travis Nieusma / Albert Cupo / Anila Yasmeen / Michael Golabek / Pavel Pugach / P J Klasse / John P Moore / Rogier W Sanders / Andrew B Ward / Ian A Wilson /
PubMed AbstractA key challenge in the quest toward an HIV-1 vaccine is design of immunogens that can generate a broadly neutralizing antibody (bnAb) response against the enormous sequence diversity of the HIV-1 ...A key challenge in the quest toward an HIV-1 vaccine is design of immunogens that can generate a broadly neutralizing antibody (bnAb) response against the enormous sequence diversity of the HIV-1 envelope glycoprotein (Env). We previously demonstrated that a recombinant, soluble, fully cleaved SOSIP.664 trimer based on the clade A BG505 sequence is a faithful antigenic and structural mimic of the native trimer in its prefusion conformation. Here, we sought clade C native-like trimers with comparable properties. We identified DU422 and ZM197M SOSIP.664 trimers as being appropriately thermostable (Tm of 63.4 °C and 62.7 °C, respectively) and predominantly native-like, as determined by negative-stain electron microscopy (EM). Size exclusion chromatography, ELISA, and surface plasmon resonance further showed that these trimers properly display epitopes for all of the major bnAb classes, including quaternary-dependent, trimer-apex (e.g., PGT145) and gp120/gp41 interface (e.g., PGT151) epitopes. A cryo-EM reconstruction of the ZM197M SOSIP.664 trimer complexed with VRC01 Fab against the CD4 binding site at subnanometer resolution revealed a striking overall similarity to its BG505 counterpart with expected local conformational differences in the gp120 V1, V2, and V4 loops. These stable clade C trimers contribute additional diversity to the pool of native-like Env immunogens as key components of strategies to induce bnAbs to HIV-1.
External linksProc Natl Acad Sci U S A / PubMed:26372963 / PubMed Central
MethodsEM (single particle)
Resolution9.32 Å
Structure data

EMDB-3059:
ZM197 SOSIP.664 trimer in complex with VRC01 Fab
Method: EM (single particle) / Resolution: 9.32 Å

Source
  • Human immunodeficiency virus 1
  • Homo sapiens (human)

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