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*
Department of Clinical Medicine, Division of Obstetrics and Gynaecology, University of Bristol, St. Michael’s Hospital, Bristol, United Kingdom; and
Department of Immunology, St. Bartholomew’s and Royal London School of Medicine and Dentistry, Queen Mary Westfield College, London, United Kingdom
HLA-F is currently the most enigmatic of the human MHC-encoded
class Ib genes. We have investigated the expression of HLA-F using a
specific Ab raised against a synthetic peptide corresponding to amino
acids 61–84 in the 
1 domain of the predicted HLA-F protein. HLA-F
is expressed as a ß2-microglobulin-associated, 42-kDa
protein that shows a restricted tissue distribution. To date, we have
detected this product only in peripheral blood B cells, B cell lines,
and tissues containing B cells, in particular adult tonsil and fetal
liver, a major site of B cell development. Thermostability assays
suggest that HLA-F is expressed as an empty heterodimer devoid of
peptide. Consistent with this, studies using endoglycosidase-H and cell
surface immunoprecipitations also indicate that the overwhelming
majority of HLA-F contains an immature oligosaccharide component and is
expressed inside the cell. We have found that IFN-
treatment induces
expression of HLA-F mRNA and HLA-F protein, but that this does not
result in concomitant cell surface expression. HLA-F associates with at
least two components of the conventional class I assembly pathway,
calreticulin and TAP. The unusual characteristics of the predicted
peptide-binding groove together with the predominantly intracellular
localization raise the possibility that HLA-F may be capable of binding
only a restricted set of peptides.
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