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Inhibitory Effect of Human Anti-CA I Autoantibodies and Development of Monoclonal Antibody mAb 2B8 Targeting Carbonic Anhydrase I

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F24%3A00604096" target="_blank" >RIV/61388971:_____/24:00604096 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216275:25310/24:39922262 RIV/00209805:_____/24:00080106

  • Result on the web

    <a href="https://onlinelibrary.wiley.com/doi/10.1155/mi/9981131" target="_blank" >https://onlinelibrary.wiley.com/doi/10.1155/mi/9981131</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1155/mi/9981131" target="_blank" >10.1155/mi/9981131</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Inhibitory Effect of Human Anti-CA I Autoantibodies and Development of Monoclonal Antibody mAb 2B8 Targeting Carbonic Anhydrase I

  • Original language description

    Spontaneous tumor regression is a recognized phenomenon across various cancer types. Recent research emphasizes the alterations in autoantibodies against carbonic anhydrase I (CA I) (anti-CA I) levels as potential prognostic markers for various malignancies. Particularly, autoantibodies targeting CA I and II appear to induce cellular damage by inhibiting their respective protein's catalytic functions. Our study illuminates the profound impact of anti-CA I autoantibodies from patient serum on the esterase activity of human CA I, exhibiting inhibitory effects akin to the acetazolamide inhibitor. Concurrently, our newly synthesized mouse monoclonal IgG antibody, mAb 2B8, against human CA I showcased a potent inhibitory action. An in-depth exploration into mAb 2B8 ' s binding dynamics with its target enzyme was undertaken. Leveraging epitope extraction and phage display library techniques, we identified the amino acid sequence DFWTYP (positions 191-196 of CA I) as crucial for mAb 2B8 ' s interaction. In 3-D structural analysis, this sequence is spatially adjacent to a previously identified epitope (DFWTYP) that interacts with patient-derived autoantibodies. Critically, mAb 2B8 demonstrated an ability to infiltrate eukaryotic cells, engaging specifically with its intracytoplasmic target. This positions mAb 2B8 as a promising model for future studies aimed at tumor cell eradication.

  • 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

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    <a href="/en/project/EF17_048%2F0007421" target="_blank" >EF17_048/0007421: Strengthening interdisciplinary cooperation in research of nanomaterials and their effects on living organisms (NANOBIO)</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2024

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Mediators of Inflammation

  • ISSN

    0962-9351

  • e-ISSN

    1466-1861

  • Volume of the periodical

    2024

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    11

  • Pages from-to

    9981131

  • UT code for WoS article

    001385412900001

  • EID of the result in the Scopus database