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The Journal of Immunology, 2007, 178: 4705.
Copyright © 2007 by The American Association of Immunologists, Inc.

LETTERS TO THE EDITOR

AAIR: Antibody Antigen Information Resource

Zhiqun Tang*, Lianyi Han*, Bin Xie*, Choong Yong Ung*, Li Jiang*, Zhiwei Cao{dagger} and Yuzong Chen*,{dagger}

* Bioinformatics and Drug Design Group Department of Pharmacy and Department of Computational Science National University of Singapore Singapore {dagger} Shanghai Center for Bioinformatics Technology Shanghai, People’s Republic of China

Antibodies recognize pathogens via sequence-specific binding to Ags (1, 2). Ab-based vaccines have been extensively explored for therapeutic applications (1, 3, 4). Molecular level information about Ab-Ag recognition is important for studying immune responses and discovering vaccines and diagnostic tools. There is a scarcity of public sources for obtaining such information, and efforts are being directed at developing such resources (5, 6).

We are pleased to introduce the Antibody Antigen Information Resource (AAIR) database (http://bidd.nus.edu.sg/group/antibody/antibody.asp), free of charge for academic use, to provide the relevant information reported in the literatures. It includes sequences and functions of Abs and Ags, source organism and strains, targeted diseases and therapeutic implications, Ab identification and production methods, and references. Entries are searchable by Ag name and source organism, Ab information (isotype, source organism, biochemical, and structural type), disease class and name, and therapeutic applications. A full list of these search items is provided on the Web page for facilitating a search. Disease classes are defined by the international classification of diseases of the World Health Organization (7).

AAIR currently contains 2546 Ab-Ag pairs covering 177 disease conditions and 614 distinct Ag sequences from various viruses, bacteria, tumor types, and autoimmune responses. Efforts are being made to collect more data. The advances in technology for identifying Ab-Ag recognitions (8) will enable the generation of more comprehensive spectrum of data that can be incorporated into the AAIR database.

References

  1. Roskos, L. K., C. G. Davis, G. M. Schwab. 2004. The clinical pharmacology of therapeutic monoclonal antibodies. Drug Dev. Res. 61: 108-120.
  2. Nussenzweig, M. C., F. W. Alt. 2004. Antibody diversity: one enzyme to rule them all. Nat. Med. 10: 1304-1305. [Medline]
  3. Pantophlet, R., D. R. Burton. 2006. GP120: target for neutralizing HIV-1 antibodies. Annu. Rev. Immunol. 24: 739-769. [Medline]
  4. Presta, L. G.. 2005. Selection, design, and engineering of therapeutic antibodies. J. Allergy Clin. Immunol. 116: 731-736; quiz 737. [Medline]
  5. Sette, A., W. Fleri, B. Peters, M. Sathiamurthy, H. H. Bui, S. Wilson. 2005. A roadmap for the immunomics of category A-C pathogens. Immunity 22: 155-161. [Medline]
  6. Singh, M. K., S. Srivastava, G. P. Raghava, G. C. Varshney. 2006. HaptenDB: a comprehensive database of haptens, carrier proteins and anti-hapten antibodies. Bioinformatics 22: 253-255. [Abstract/Free Full Text]
  7. World Health Organization 1992. International Statistical Classification of Diseases and Related Health Problems World Health Organization, Geneva.
  8. Preuss, K. D., C. Zwick, C. Bormann, F. Neumann, M. Pfreundschuh. 2002. Analysis of the B cell repertoire against antigens expressed by human neoplasms. Immunol. Rev. 188: 43-50. [Medline]




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