Abstract
Molecular mimicry defines similar structures shared by molecules from dissimilar genes or by their protein products. Either the molecules’ linear amino acid sequences or their conformational fit may be shared, even though their origins are as separate as, for example, a virus and a normal host self determinant. Because guanine-cytosine (GC) sequences and introns designed to be spliced away may provide, respectively, false hybridization signals and nonsense homologies, we focus here on molecular mimicry at the protein level. Such homologies between proteins have been detected either by use of immunologic reagents, humoral or cellular, that cross-react with two presumably unrelated protein structures, or by computer searches to match proteins described in storage banks. Regardless of the methods used for identification, it is now clear that molecular mimicry between proteins encoded by numerous DNA and RNA viruses and host “self” proteins is a relatively common event [1–3]. Among the broad implications of these data are leads for understanding virally induced autoimmunity and disease [2–8] as well as mechanisms by which viral proteins are processed inside cells [9]. Further, the,unexpected cross-reactivities attendant to mimicry warrant cautious use or reagents in diagnostic virology and microbiology, even though these materials originated from hybridomas or from animals immunized with predetermined (peptide) amino acid sequences.
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Keywords
- Myelin Basic Protein
- Molecular Mimicry
- Viral Pathogenesis
- Japanese Encephalitis Virus
- Human Respiratory Syncytial Virus
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
References
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Oldstone, M.B.A., Notkins, A.L. (1986). Molecular Mimicry. In: Notkins, A.L., Oldstone, M.B.A. (eds) Concepts in Viral Pathogenesis II. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-4958-0_23
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