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*
The Biomedical Research Centre, University of British Columbia, Vancouver, British Columbia, Canada; and
Division of Hematology/Oncology, Tupper Research Institute, New England Medical Center, Boston, MA 02111
The mAb 1B11 has been characterized as recognizing the
activation-associated glycoform of murine CD43, a heavily
O-glycosylated protein implicated in leukocyte homing.
When hemopoietic cells from CD43-/- mice were stained
with 1B11, CD43-independent binding of 1B11 was observed on peripheral
CD8 T cells and at low levels on thymocytes, while no binding was
detected on CD4 T cells, B cells, or bone marrow cells. Levels of 1B11
staining were comparable in lymph node CD8+ T cells from
both CD43-/- mice and CD43+/+ mice. We sought
to identify the CD43-independent target of 1B11 expressed on CD8 T
cells. Previous work had demonstrated that neuraminidase treatment of
lymph node cells (LNC) enhanced 1B11 binding on CD43+/+
LNC; this enhancement was also observed in CD43-/- LNC.
We show that neuraminidase-enhanced 1B11 binding in
CD43-/- LNC and EL4 thymoma cells is CD43 independent and
that 1B11 detects a novel target of apparent mass of 
200 kDa
identified as a hyposialylated form of CD45RB preferentially expressed
on peripheral CD8, but not CD4, T cells. Our data also show that the
recognition of CD43 and CD45RB by 1B11 is differentially affected by
O-linked glycosylation and sialic acid. Whereas 1B11
recognition of CD43 on activated T cells required both core 2
O-glycan branching and sialic acid, 1B11 recognition of
CD45 only occurred in the absence of both core 2 glycosylation and
sialic acid.
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