scholarly journals Clonal Distribution and Phase-Variable Expression of a Major Histocompatibility Complex Analogue Protein in Staphylococcus aureus

2005 ◽  
Vol 187 (8) ◽  
pp. 2917-2919 ◽  
Author(s):  
Angus Buckling ◽  
James Neilson ◽  
Jodi Lindsay ◽  
Richard ffrench-Constant ◽  
Mark Enright ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Major Histocompatibility Complex ◽  
Allelic Variant ◽  
Phase Variable ◽  
Major Histocompatibility ◽  
Variable Expression ◽  
Histocompatibility Complex ◽  
Complex Analogue ◽  
Clonal Distribution

ABSTRACT The mapW gene of Staphylococcus aureus strain N315 contains a poly(A) tract which truncates translation of the protein. This study demonstrates that mapW is an allelic variant of the map/eap genes found in other strains and that the variation in the length of this poly(A) tract suggests that it is a contingency locus.

scholarly journals Defective intracellular transport as a common mechanism limiting expression of inappropriately paired class II major histocompatibility complex alpha/beta chains.

1991 ◽  
Vol 174 (4) ◽  
pp. 799-808 ◽  
Author(s):  
A J Sant ◽  
L R Hendrix ◽  
J E Coligan ◽  
W L Maloy ◽  
R N Germain
Keyword(s):  
Major Histocompatibility Complex ◽  
Intracellular Transport ◽  
Surface Expression ◽  
Class Ii ◽  
Common Mechanism ◽  
Major Histocompatibility ◽  
Variable Expression ◽  
Histocompatibility Complex ◽  
Alpha Beta ◽  
Endoglycosidase H

Distinct combinations of class II major histocompatibility complex (MHC) alpha and beta chains show widely varying efficiencies of cell surface expression in transfected cells. Previous studies have analyzed the regions of the class II chains that are critically involved in this phenomenon of variable expression and have shown a predominant effect of the NH2-terminal domains comprising the peptide-binding site. The present experiments attempt to identify the post-translational defects responsible for this variation in surface class II molecule expression for both interisotypic alpha/beta combinations failing to give rise to any detectable cell membrane molecules (e.g., E alpha A beta k) and intraisotypic pairs with inefficient surface expression (e.g., A alpha d A beta k). The results of metabolic labeling and immunoprecipitation experiments using L cell transfectants demonstrate that in both of these cases, the alpha and beta chains form substantial amounts of stable intracellular dimers. However, the isotype- and allele-mismatched combinations do not show the typical post-translational increases in molecular weight that accompany maturation of the N-linked glycans of class II MHC molecules. Studies with endoglycosidase H reveal that no or little progression to endoglycosidase H resistance occurs for these mismatched dimers. These data are consistent with active or passive retention of relatively stable and long-lived mismatched dimers in a pre-medial-Golgi compartment, possibly in the endoplasmic reticulum itself. This retention accounts for the absent or poor surface expression of these alpha/beta combinations, and suggests that conformational effects of the mismatching in the NH2-terminal domain results in a failure of class II molecules to undergo efficient intracellular transport.

scholarly journals Use of Peptide-Major Histocompatibility Complex Tetramer Technology To Study Interactions between Staphylococcus aureus Proteins and Human Cells

2007 ◽  
Vol 75 (12) ◽  
pp. 5711-5715 ◽  
Author(s):  
Ruth C. Massey ◽  
Thomas J. Scriba ◽  
Eric L. Brown ◽  
Rodney E. Phillips ◽  
Andrew K. Sewell
Keyword(s):  
Staphylococcus Aureus ◽  
Major Histocompatibility Complex ◽  
Mhc Class Ii ◽  
Cell Receptor ◽  
Major Histocompatibility ◽  
Toxic Shock ◽  
Histocompatibility Complex ◽  
Amino Acid Repeats ◽  
Receptor Interactions ◽  
Toxic Shock Syndrome Toxin

ABSTRACT In this study, we report the use of peptide-major histocompatibility complex tetramer technology to study the interactions that occur between Staphylococcus aureus proteins and human leukocytes. We demonstrated that this technology can be used to study the activity of superantigens such as toxic shock syndrome toxin 1 and also found that despite similarities to known proteins (i.e., major histocompatibility complex [MHC] class II molecules and superantigens), the S. aureus Eap protein does not block MHC-T-cell receptor interactions and is not a superantigen. Instead, it has nonspecific cross-linking activity that is dependent upon having at least two of its six 110-amino-acid repeats.

Relationship of Major Histocompatibility Complex Class II Genes to Inhibitor Antibody Formation in Hemophilia A

1990 ◽  
Vol 64 (04) ◽  
pp. 564-568 ◽  
Author(s):  
Lloyd E Lippert ◽  
Lyman Mc A Fisher ◽  
Lawrence B Schook
Keyword(s):  
Major Histocompatibility Complex ◽  
Factor Viii ◽  
Antibody Formation ◽  
Rflp Analysis ◽  
Class Ii ◽  
Major Histocompatibility ◽  
Odds Ratios ◽  
Inhibitory Antibody ◽  
Histocompatibility Complex ◽  
Hla Dr

SummaryApproximately 14% of transfused hemophiliacs develop an anti-factor VIII inhibitory antibody which specifically neutralizes factor VIII procoagulant activity. In this study an association of the major histocompatibility complex (MHC) with inhibitor antibody formation was evaluated by restriction fragment length polymorphism (RFLP) analysis using BamHI, EcoRI, HindII, PstI, PvuII and TaqI digested genomic DNA probed with DP beta, DQ alpha, DQ beta and DR beta class II MHC gene probes. The RFLP patterns for 16 non-inhibitor and 11 inhibitor hemophiliac patients were analyzed. These 24 enzyme:probe combinations generated 231 fragments. Fifteen (15) fragments associated with the inhibitor phenotype; odds ratios ranged from 5.1 to 45 and lower bounds of 95% confidence intervals were > 1.000 for all 15 fragments. Five (5) fragments associated with non-inhibitors, with odds ratios ranging from 6.4 to 51.7. This report establishes a MHC related genetic basis for the inhibitor phenotype. No statistically significant differences in the distribution of serologically defined HLA-DR phenotypes were observed between the inhibitor and non-inhibitor groups.

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