Heavy-chain antibody

Source: Wikipedia, the free encyclopedia.

A heavy-chain antibody is an antibody which consists only of two heavy chains and lacks the two light chains usually found in antibodies.

In common antibodies, the

single-domain antibodies.[1]

Discovery

In 1989 a group of biologists led by

dromedaries. In addition to the expected four-chain antibodies, they identified simpler antibodies consisting only of two heavy chains. This discovery was published in Nature in 1993.[2] In 1995 a research team at the University of Miami found a different type of heavy-chain antibodies in sharks.[3]

In cartilaginous fishes

A heavy-chain shark antibody (left) and a heavy-chain camelid antibody (middle) in comparison to a common antibody (right). Heavy chains are shown in a darker shade, light chains in a lighter shade.

The immunoglobulin new antigen receptor (IgNAR) of

Non-vertebrates
do not have antibodies at all.

Sharks, and possibly other cartilaginous fishes, have immunoglobulin M (IgM) and immunoglobulin W (IgW) as well, both types with two heavy and two light chains.[5]

In camelids

The only mammals with heavy-chain (

conformation of the CDR1. It has been reasoned that these similarities are caused by functional requirements, or convergent evolution, rather than a genuine relationship.[4]

About 50% of the antibodies in camelids are of the ordinary mammalian heavy/light-chain type.[7] It is not known whether any type of animal has only heavy-chain antibodies and completely lacks the common type with two heavy and two light chains.

Heavy-chain camelid antibodies have been found to be just as specific as a regular antibody and in some cases they are more robust. As well, they are easily isolated using the same phage panning procedure used for traditional antibodies, allowing them to be cultured

SARS-CoV-2 and other virus infections.[citation needed] The smaller size and single domain make these antibodies easier to transform into bacterial cells for bulk production, making them ideal for research purposes.[8]

References

  1. ^
    PMID 17704915
    .
  2. ^
    S2CID 4265902
    .
  3. S2CID 4304231
    .
  4. ^
    S2CID 25137728
    .
  5. PMID 19554288
    .
  6. PMID 12543123
    .
  7. ^ "Nanobodies". Nanobody.org. 2006.
  8. ^ Ghannam, A., Kumari, S., Muyldermans, S., & Abbady, A. Q. (2015). Camelid nanobodies with high affinity for broad bean mottle virus: a possible promising tool to immunomodulate plant resistance against viruses. Plant Molecular Biology, 1-15.

External links

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