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During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
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Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
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Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
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The HIV-1 gp120 V1V2 loop: structure, function and importance for vaccine development.

Robert J O'Connell1, Jerome H Kim, Jean-Louis Excler

  • 1Armed Forces Research Institute of Medical Sciences (AFRIMS), 315/6 Rajvithi Road, Bangkok 10400, Thailand.

Expert Review of Vaccines
|August 29, 2014
PubMed
Summary

Boosting antibodies against the HIV-1 V2 domain may enhance vaccine efficacy. Increased anti-V2 responses correlate with reduced HIV-1 acquisition risk, suggesting a key target for future vaccine strategies.

Keywords:
HIV vaccineRV144V1V2 loopefficacygp120neutralizing antibodiesnonneutralizing antibodies

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Area of Science:

  • Immunology
  • Virology
  • Vaccinology

Background:

  • The HIV-1 gp120 envelope glycoprotein's V2 loop, despite sequence diversity, maintains critical structural and sequence conservation.
  • V2 is crucial for HIV-1 entry, influencing trimer stability and co-receptor binding.
  • V2 is a key target for broadly neutralizing antibodies and a site of immune evasion via sequence and glycosylation variation.

Purpose of the Study:

  • To investigate the role of vaccine-induced antibodies targeting the HIV-1 V2 domain in protection against HIV-1 acquisition.
  • To evaluate the correlation between anti-V2 antibody responses and HIV-1/SIV acquisition in vaccine trials and challenge studies.
  • To hypothesize the impact of enhanced anti-V2 antibody responses on the efficacy of pox-protein prime-boost HIV vaccine strategies.

Main Methods:

  • Analysis of antibody responses in the RV144 HIV-1 vaccine trial.
  • Examination of HIV-1 strains from vaccine and placebo recipients.
  • Assessment of non-human primate challenge studies with simian immunodeficiency virus (SIV).

Main Results:

  • Vaccine-induced IgG against V1V2 inversely correlated with HIV-1 acquisition risk in the RV144 trial.
  • HIV-1 strains from RV144 vaccine recipients showed differences in the V2 domain compared to placebo recipients.
  • Non-human primate studies showed an inverse correlation between anti-V2 responses and SIV acquisition.

Conclusions:

  • The V2 domain is a critical target for protective HIV-1 vaccine strategies.
  • Enhancing the magnitude, frequency, and duration of vaccine-induced anti-V2 antibody responses may improve HIV vaccine efficacy.
  • Pox-protein prime-boost strategies could be optimized by focusing on robust anti-V2 immune responses.