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Review
. 2013 Jul;8(4):326-32.
doi: 10.1097/COH.0b013e328361d178.

Progress in HIV-1 vaccine development

Barton F Haynes  1 , M Juliana McElrath
Affiliations
Review

Progress in HIV-1 vaccine development

Barton F Haynes et al. Curr Opin HIV AIDS. 2013 Jul.

Abstract

Purpose of review: In this review, examples of recent progress in HIV-1 vaccine research are discussed.

Recent findings: New insights from the immune correlates analyses of the RV144 efficacy trial have accelerated vaccine development with leads to follow in nonhuman primate studies and improved vaccine designs. Several new vaccine vector approaches offer promise in the exquisite control of acute infection and in improving the breadth of T-cell responses. New targets of broadly neutralizing antibodies (BnAbs) have been elucidated, and improved understanding of how the human host controls BnAb development have emerged from BnAb knock-in mice and from analyses of BnAb maturation and virus evolution in individuals followed from the time of HIV-1 transmission to BnAb induction.

Summary: Based on these observations, it is clear that the development of a successful HIV-1 vaccine will require new vaccine approaches and iterative testing of immunogens in well designed animal and human trials.

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Figures

Figure 1
Figure 1
Structures of Antibodies CH58 and CH59 Bound to an HIV-1 gp120 V2 Peptide Compared to V1V2 BnAb PG9 bound to a V1V2 scaffold. RV144 vaccine-elicited antibodies CH58 and CH59 recognize alternative conformations of V2 compared to BnAb PG9.(A). Ribbon representation of the CH58 antigen-binding fragment in complex with an A244 V2 peptide as viewed end on looking at the Fab antibody conforming site. Heavy chain is colored orange, light chain is blue, and V2 peptide is green. The sequence of the peptide is shown, with modeled residues in green. The side chains of residues involved in hydrogen bonds or salt bridges are shown as sticks, with the interactions depicted as dashed lines.(B) Structure of CH59 in complex with peptide, depicted as in (A). The heavy chain is tan, and the light chain is light blue.(C) Structure of BnAb PG9 in complex with the V1V2 domain from HIV-1 strain CAP45. The PG9 structure is shown as ribbons with heavy and light chains (colored yellow and blue, respectively) in the same orientation as in (A) and (B). The V1V2 domain is shown as a gray ribbon with residues 168–176 colored green and N-linked glycans attached to residues Asn156 and Asn160 shown as sticks. Reprinted with permission from ref. [3].
Figure 2
Figure 2
A model of the HIV-1 Env spike with select BnAbs Fab molecules bound to Env BnAb binding sites. Adapted with permission from ref. [49].
See this image and copyright information in PMC

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