ok, prev post:
>>In article <ralph.1152923375B at 128.196.137.12> Ralph M Bernstein,
>>ralph at ccit.arizona.edu writes:
>>>the processing and presentation of an _epitope_, such as in the case of
>>our
>>>work, natural human autoantibodies, may be frame work1 peptides, etc-
>>never
>>>the whole idiotype. again, b cells cannot read.
perret responds
>Ab variable region is due to rearrangement and therefore different aa
>structure. It is true this is folded into a 3d structure which interacts
>with the Ag. But why can this aa sequence not be presented via the MHC
>in small peptides and elicit an immune response since they are novel
>sequences.? Remember T cells are able to distinguish single aa changes
>in small peptides. It is an intriquing question.
ok, 1) it can. but this _is not the idiotope_ that is made up of the 3d
structure-not a peptide seq.
2) these frameworks and cdrs/hvrs can be presented individually as
peptides, linear peptides, but that is all they are, not the idiotope. that
is what fuchs seems to be saying/said, and is (according to the latest data,
etc) pretty much wrong. some of these peptides can, and _do_ elicit an
immune response, but only against the frameworks and cdrs that are
_obviously_ exposed to the solution (for some interesting background
answers/reading -see any marchalonis, et al., paper in last 5 years where
the autoantibodies to a particular tcr (jurkat) and how they map and
coorespond to only those exposed in solution are shown.) so anyway, that
was the point of that post. only if somehow the limits of peptide length
and size of mhcI and II could be overcome, allowing them to present
"peptides" around approx. 40-60 aa's, with the appropriate b-barrels,
a-helices, etc, then we would be cookin. well, regards, ralph
Ralph M. Bernstein
Dept of Micro/Immuno
University of Arizona
Ph: 602 626 2585
Fx: 602 626 2100
