Describe in details the four main processes by which antibody diversity is generated in development of...

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Describe in details the four main processes by which antibody diversity is generated in development of...

Describe in details the four main processes by which antibody diversity is generated in development of the B cell repertoire. explain how these processes create more diversity in VH CDR3 than in VL CDR3 or in VH CDR2.

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used in immune responses of inbred mice to many hap- ten, polysaccharide, and even protein antigens, includ- ing p-azophenylarsonate (Pawlak et al., 1973; Makela et al., 1976; Manser, 1990), phenyloxazolone (Makela et al., 1978; Kaartinen et al, 1983; Berek and Milstein, 1987), (4-hydroxy-3 - nitrophenyl)acetyl (NP) (Imanishi and Makela, 1974, 1975; Blier and Bothwell, 1988), DNP (Dzierzak et al., 1980, 1985), phosphorylchol ine (Potter and Lieberman, 1970; Sher and Cohn, 1972; Barstad et with the findings that murine B cells that have a re- arranged heavy chain immunoglobulin gene in the germ line always change the CDR3 sequence and often the V as well when they deviate from the original antigen reactivity (Cascalho et al., 1996; López-Maclas et al., 1999). Our data may explain the long-standing puzzle of "canonical" CDR structures in antibodies (Chothia and Lesk, 1987; Chothia et al., 1989). We would suggest that uniform CDR shapes are important for the stability of a binding site, with the exception of V CDR3, which has to "fit" the antigen surface much more precisely. al., 1974; Crews et al., 1981), phosphatidylcholine (Seidl et al., 1997), dextran (Blomberg et al., 1972; Riblet et The nese results a tuctural anal- ysis shows that about 30 side chains from each protein centor whe Potter, 1978), Staphvlococcal nuclease (Fathman et al. 1977), and influenza hemagglutinin (McKean et al., 1984; Clarke et al., 1985). T cell recognition of peptide/MHC complexes is often (but not always) fairly restricted with respect to However, it is not clear whether the preferred V gene segment(s) are absolutely required for such epitopes or are merely the result of extensive clonal expansion where a slight advantage in binding would allow the most optimal VV combination to predominate. In the current study, we find that mice having only one func- tional VHand (effectively) two Vi gene segments are able Lit are in close contact but only a fraction of those residues have any contribution to the binding affinity and only two account for more than three-quarters of the free energy (Wells, 1996). Another interesting issue raised by the data presented here is the role of somatic mutation in producing higher- affinity antibodies upon rechallenge with antigen. Our data shows that, at least for protein antigens, having an arbitrarily chosen human V and one of two mouse A chains as a germl ine repertoire is no barrier to generat gene usage (e.g., Hedrick et al., 1988). sistont k on the chicken i is finding is con- where only a sing le functional V and V are utilized, but goes beyond this in two important respects. One is that most m likly that the restricted V es. to mount usage observed in most immune responses represents the consequence of antigen-driven clonal expansion of kinetically favorable In the HC1+/ lgH Igkmice, we find a remarkable restriction in V CDR3 diversity with respect to both length and amino acid composition in the primary im- mune response to both h

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