Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P01889 (ankylosing spondylitis)
 5,717 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The complete amino acid sequence of papain-solubilized HLA-B27, an antigen that presents a very strong association to the development of ankylosing spondylitis, has been determined. The overall sequence homology with the cross-reactive allelic products HLA-B7 and HLA-B40 (Bw60) is 93% and 92%, respectively. Half of the differences between HLA-B27 and -B7 are located in segments 63-83 and 113-116. Most of the known HLA class I antigens are different in these segments, and it is suggested that the corresponding residues may be involved in the alloantigenic determinants of HLA-B27. A free cysteine residue is present at position 67, and it is at least partially exposed to solvent. In addition, other differences are found in various areas of the two N-terminal domains. The comparison with available HLA class I sequences allows an evaluation of their contribution to the antigenic polymorphism of these molecules. The relevance of these data is discussed in connection with the mapping of functional sites of HLA class I antigens and with the association between HLA-B27 and ankylosing spondylitis.
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PMID:Primary structure of papain-solubilized human histocompatibility antigen HLA-B27. 240 63

A component of the cell walls of certain enteric bacteria has been identified that cross-reacts with an HLA-B27-associated cell-surface structure on lymphocytes and other cell types from patients with ankylosing spondylitis. This component, or "modifying factor," from one particular organism, Klebsiella K43-BTS1, has been studied in detail. A purification scheme has been developed using preparative electrofocusing and gel-permeation high performance liquid chromatography techniques and the purified material used in various characterization studies. A previous study demonstrated that the modifying factor has an approximate molecular weight of 30,000 and an isoelectric point of 5.4-5.5. In this study two-dimensional gel electrophoresis experiments demonstrated that the modifying factor is associated with a single protein component of the cell wall of this organism. Pronase and papain destroyed the modifying factor activity whereas trypsin and alpha-chymotrypsin degraded the factor into smaller fragments without destroying its ability to modify B27+ AS- lymphocytes. Neuraminidase did not affect the modifying factor itself but did affect B27+ AS- lymphocytes such that they became unresponsive to modification. Sugar inhibition studies suggested that sugar groups are probably not involved in the function of the modifying factor. The availability of purified modifying factor should permit more detailed chemical analyses as well as functional studies to determine the significance of this molecule to the pathogenesis of ankylosing spondylitis.
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PMID:Biochemical studies on a factor isolated from Klebsiella K43-BTS1 that cross-reacts with cells from HLA-B27 positive patients with ankylosing spondylitis. 353 95