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Proteins mimicking epitope of HIV-1 virus neutralizing antibody induce virus-neutralizing sera in mice

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00027162%3A_____%2F19%3AN0000356" target="_blank" >RIV/00027162:_____/19:N0000356 - isvavai.cz</a>

  • Alternative codes found

    RIV/86652036:_____/19:00511409 RIV/61989592:15110/19:73596349 RIV/00027162:_____/19:N0000216

  • Result on the web

    <a href="https://www.sciencedirect.com/science/article/pii/S2352396419304505" target="_blank" >https://www.sciencedirect.com/science/article/pii/S2352396419304505</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.ebiom.2019.07.015" target="_blank" >10.1016/j.ebiom.2019.07.015</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Proteins mimicking epitope of HIV-1 virus neutralizing antibody induce virus-neutralizing sera in mice

  • Original language description

    Background The development of an effective vaccine preventing HIV-1 infection is hindered by the enormous antigenic variability and unique biochemical and immunological properties of HIV-1 Env glycoprotein, the most promising target for HIV-1 neutralizing antibody. Functional studies of rare elite neutralizers led to the discovery of broadly neutralizing antibodies. Methods We employed a highly complex combinatorial protein library derived from a 5 kDa albumin-binding domain scaffold, fused with support protein of total 38 kDa, to screen for binders of broadly neutralizing antibody VRC01 paratope. The most specific binders were used for immunization of experimental mice to elicit Env-specific antibodies and to test their neutralization activity using a panel of HIV-1 clade C and B pseudoviruses. Findings Three most specific binders designated as VRA017, VRA019, and VRA177 exhibited high specificity to VRC01 antibody. Immunized mice produced Env-binding antibodies which neutralize eight of twelve HIV-1 Tier 2 pseudoviruses. Molecular modelling revealed a shape complementarity between VRA proteins and a part of VRC01 gp120 interacting surface. Interpretation This strategy based on the identification of protein replicas of broadly neutralizing antibody paratope represents a novel approach in HIV-1 vaccine development. This approach is not affected by low immunogenicity of neutralization-sensitive epitopes, variability, and unique biochemical properties of HIV-1 Env used as a crucial antigen in the majority of contemporary tested vaccines.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    30102 - Immunology

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2019

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    EBIOMEDICINE

  • ISSN

    2352-3964

  • e-ISSN

  • Volume of the periodical

    47

  • Issue of the periodical within the volume

    September 2019

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    10

  • Pages from-to

    247-256

  • UT code for WoS article

    000486976200036

  • EID of the result in the Scopus database

    2-s2.0-85072567469