Monoclonal Antibodies Specific for Llama and Alpaca IgG1, IgG2 and IgG3
- Others
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Daley LP, Gagliardo LF, Duffy MS, Smith MC, Appleton JA (2005) Application of monoclonal antibodies in function and comparative investigations of heavy-chain immunoglobulins in new world camelids. Clin Diagn Lab Immunol. 12(3):380-6.
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1065209
- *Abstract
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Camelid IgG2 and IgG3 are distinguished from conventional IgGs, in that they do not associate with light chains; as such they are called heavy-chain antibodies (HCAbs).
These HCAbs have unusual properties including extended hinge regions, deletion of the CH1 domain, and substitutions in amino acids within the V domain, making HCAbs more hydrophilic to promote flexibility and solubility. These distinctions allow HCAbs to bind less accessible epitopes, thus increasing their antigen-binding abilities and therapeutic potential.
Furthermore because HCAbs lack light chains, only the heavy chain is responsible for binding an epitope. The extended complementarity-determining regions (CDR) of HCAbs can insert into the active site of enzymes inhibiting their activity. It is likely that HCAbs play a novel role in immune defense.
Here investigators have produced isotype specific mouse monoclonal antibodies, which can be used to investigate the roles of HCAbs in camelid immunity. These are the first monoclonal specific antibodies that have been characterized and documented to be specific for llama and alpaca IgG1, IgG2, and IgG3. These unique binding characteristics combined with the ease of production make these antibodies promising immunological tools.
- *Licensing
- Phillip Owhpo62@cornell.edu607-254-4508
- Country/Region
- USA
