Glycobiology, Vol 9, 267-275, Copyright © 1999 by Oxford University Press
E Ümit Bagriaçik and KS Miller
It has been known for over a decade that sialidase (neuraminidase)
treatment could substantially enhance the capacity of resting B cells to
stimulate the proliferation of allogeneic and antigen specific, syngeneic T
cells. Thus, cell-surface sialic acid was implicated as a potential
modulator of immune cell interaction. However, little progress has been
made in either identifying explicit roles for sialic acid in this system or
in hypothesizing mechanisms to explain the "neuraminidase effect." Here we
show for the first time that cell surface sialic acid on medium incubated B
cells blocks access to costimulatory molecules on the B cell surface, and
that this is the most likely explanation for the neuraminidase effect.
Further, we show that it is likely to be upregulation of ICAM-1 and its
subsequent engagement of LFA-1 rather than loss of cell surface sialic acid
that in part regulates access to CD86 and other costimulatory molecules.
However, we cannot exclude a role for CD86-bound sialic acid on the B cell
in modulating binding to T cell CD28. Because sialidase treatment of
resting B cells but not resting T cells enables T cell activation, we
suggest that sialidase treatment may still be an analogue for an authentic
step in B cell activation, and show that for highly activated B cells
(activated with polyclonal anti-IgM plus INF-gamma) there is specific loss
2, 6-linked sialic acid. Potential roles for sialic acid in modulating B
cell/T cell collaboration are discussed.
ORIGINAL ARTICLES
Cell surface sialic acid and the regulation of immune cell interactions: the neuraminidase effect reconsidered
Faculty of Biological Science and The Mervin Bovaird Center for Studies in Molecular Biology and Biotechnology, The University of Tulsa, Tulsa,OK 74104, USA.
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