Evidence map›Paper›PMID 16699036›Full record

ArticleJournal of virology2006

Sequential immunization with V3 peptides from primary human immunodeficiency virus type 1 produces cross-neutralizing antibodies against primary isolates with a matching narrow-neutralization sequence motif.

Yasuyuki Eda, Mari Takizawa, Toshio Murakami, Hiroaki Maeda, Kazuhiko Kimachi, Hiroshi Yonemura, Satoshi Koyanagi, Kouichi Shiosaki, Hirofumi Higuchi, Keiichi Makizumi and 6 more

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
0.9field-weighted citation impact, top 30% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed, 55 citations in OpenAlex.

  1. Peptides for Vaccine Development.ACS applied bio materials · 2022
    Review
  2. Article
  3. Review
  4. Specific Substitutions in Region V2 of gp120Pathogens (Basel, Switzerland) · 2020
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Progress toward active or passive HIV-1 vaccination.The Journal of experimental medicine · 2017
    Review
  13. Article
  14. Article
  15. Molecular recognition of human ephrinB2 cell surface receptor by an emergent African henipavirus.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  16. Structural basis of clade-specific HIV-1 neutralization by humanized anti-V3 monoclonal antibody KD-247.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015
    Article
  17. Article
  18. Review
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

16 authors at 4 institutions in 1 country.

Yasuyuki EdaAIDS Research Center, National Institute of Infectious Diseases, Shinjuku-ku, Tokyo 162-8640, Japan.
Mari Takizawa
Toshio Murakami
Hiroaki Maeda
Kazuhiko Kimachi
Hiroshi Yonemura
Satoshi Koyanagi
Kouichi Shiosaki
Hirofumi Higuchi
Keiichi Makizumi
Toshihiro Nakashima
Kiyoshi Osatomi
Sachio Tokiyoshi
Shuzo Matsushita
Naoki Yamamoto
Mitsuo Honda
Kaketsuken (Japan) · JPNational Institute of Infectious Diseases · JPKumamoto University · JPNagasaki University · JP

Funding

VIROLOGY COREP30AI027742 · NIAID · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI GORNY, MIROSLAW K · 1989 to 2010
$19.4M
NIAID NIH HHS AI 27742NIAID NIH HHS P30 AI027742
6 · The paper itself

Abstract

An antibody response capable of neutralizing not only homologous but also heterologous forms of the CXCR4-tropic human immunodeficiency virus type 1 (HIV-1) MNp and CCR5-tropic primary isolate HIV-1 JR-CSF was achieved through sequential immunization with a combination of synthetic peptides representing HIV-1 Env V3 sequences from field and laboratory HIV-1 clade B isolates. In contrast, repeated immunization with a single V3 peptide generated antibodies that neutralized only type-specific laboratory-adapted homologous viruses. To determine whether the cross-neutralization response could be attributed to a cross-reactive antibody in the immunized animals, we isolated a monoclonal antibody, C25, which neutralized the heterologous primary viruses of HIV-1 clade B. Furthermore, we generated a humanized monoclonal antibody, KD-247, by transferring the genes of the complementary determining region of C25 into genes of the human V region of the antibody. KD-247 bound with high affinity to the "PGR" motif within the HIV-1 Env V3 tip region, and, among the established reference antibodies, it most effectively neutralized primary HIV-1 field isolates possessing the matching neutralization sequence motif, suggesting its promise for clinical applications involving passive immunizations. These results demonstrate that sequential immunization with B-cell epitope peptides may contribute to a humoral immune-based HIV vaccine strategy. Indeed, they help lay the groundwork for the development of HIV-1 vaccine strategies that use sequential immunization with biologically relevant peptides to overcome difficulties associated with otherwise poorly immunogenic epitopes.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsCross ReactionsEpitopesHIV-1HIV AntibodiesHIV Envelope Protein gp120HumansMiceNeutralization TestsPeptide FragmentsEpitopesHIV AntibodiesHIV Envelope Protein gp120Peptide Fragments

Identifiers

PMID16699036
PMCPMC1472165
OpenAlexW2164094123

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.