Natural monoclonal antibody to oxidized low-density lipoprotein and Aggregatibacter actinomycetemcomitans

Wang, Chunguang; Hörkkö, Sohvi (2017-07-01)
 
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URL:
https://doi.org/10.1007/978-1-4939-7180-0_12

Wang, Chunguang
Hörkkö, Sohvi
Humana Press
01.07.2017

Wang C., Hörkkö S. (2017) Natural Monoclonal Antibody to Oxidized Low-Density Lipoprotein and Aggregatibacter actinomycetemcomitans. In: Kaveri S., Bayry J. (eds) Natural Antibodies. Methods in Molecular Biology, vol 1643. Humana Press, New York, NY

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© Springer Science+Business Media LLC 2017. This is a post-peer-review, pre-copyedit version of an article published in Natural Antibodies. Methods in Molecular Biology. The final authenticated version is available online at: https://doi.org/10.1007/978-1-4939-7180-0_12.
https://rightsstatements.org/vocab/InC/1.0/
doi:https://doi.org/10.1007/978-1-4939-7180-0_12
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https://urn.fi/URN:NBN:fi-fe2019082926063
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Abstract

Natural antibodies are produced by B lymphocytes without exogenous antigenic exposure and are present at the time of birth. They usually bind to conserved epitopes on antigens of different chemical compositions. We cloned and characterized a natural mouse monoclonal IgM antibody (Aa_Mab) by selecting the binding to malondialdehyde acetaldehyde (MAA) adducts on low-density lipoprotein (LDL). The data showed that the Aa_Mab cross-reacted with Aggregatibacter actinomycetemcomitans (Aa) bacteria, an important oral pathogen in periodontitis associated with atherosclerosis. Surprisingly, the binding molecule of Aa bacteria to the Aa_Mab was Aa chaperonin 60 or HSP60, a protein that is not only responsible for maintaining cellular proteins conformation, but also functions as a potent virulence factor prompting bone resorption in periodontitis and as a putative pathogenic factor in atherosclerosis.

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