Amino acid comparison of the class I antigens of mouse major histocompatibility complex

1989 ◽  
Vol 30 (5) ◽  
pp. 390-392 ◽  
Author(s):  
Suzanne Watts ◽  
Christopher Wheeler ◽  
Roxanne Morse ◽  
Robert S. Goodenow
Keyword(s):  
Major Histocompatibility Complex ◽  
Amino Acid ◽  
Class I ◽  
Major Histocompatibility ◽  
Mouse Major Histocompatibility Complex ◽  
Histocompatibility Complex ◽  
Amino Acid Comparison ◽  
Acid Comparison

scholarly journals Presentation of numerous viral peptides to mouse major histocompatibility complex (MHC) class I-restricted T lymphocytes is mediated by the human MHC-encoded transporter or by a hybrid mouse-human transporter.

1993 ◽  
Vol 177 (6) ◽  
pp. 1785-1790 ◽  
Author(s):  
J W Yewdell ◽  
F Esquivel ◽  
D Arnold ◽  
T Spies ◽  
L C Eisenlohr ◽  
...  
Keyword(s):  
T Cells ◽  
Major Histocompatibility Complex ◽  
Antigen Processing ◽  
Class I ◽  
Gene Products ◽  
Major Histocompatibility ◽  
Mouse Major Histocompatibility Complex ◽  
Histocompatibility Complex ◽  
Functional Complex ◽  
Human And Mouse

The major histocompatibility complex-encoded transporter associated with antigen processing (TAP) is required for the efficient presentation of cytosolic antigens to class I-restricted T cells. TAP is thought to be formed by the interaction of two gene products, termed TAP1 and TAP2. We find that TAPs consisting either of human subunits, or mouse TAP1 and human TAP2, facilitate the presentation of numerous defined viral peptides to mouse class I-restricted T cells. As human and mouse TAP2 and TAP1 differ in 23 and 28% of their residues, respectively, this indicates that TAP1 and TAP2 can form a functional complex with partners considerably different from those they coevolved with. Moreover, these findings indicate that widely disparate TAPs facilitate delivery of the same peptides to class I molecules. These findings suggest that TAP polymorphism does not greatly influence the types of peptides presented to the immune system.

scholarly journals Evidence that gene G7a in the human major histocompatibility complex encodes valyl-tRNA synthetase

1991 ◽  
Vol 278 (3) ◽  
pp. 809-816 ◽  
Author(s):  
S L Hsieh ◽  
R D Campbell
Keyword(s):  
Major Histocompatibility Complex ◽  
Amino Acid ◽  
Molecular Mass ◽  
Trna Synthetase ◽  
Class I ◽  
Major Histocompatibility ◽  
High Sequence Identity ◽  
Human Major Histocompatibility Complex ◽  
Trna Synthetases ◽  
Histocompatibility Complex

At least 36 genes have now been located in a 680 kb segment of DNA between the class I and class II multigene families within the class III region of the human major histocompatibility complex on chromosome 6p21.3. The complete nucleotide sequence of the 4.3 kb mRNA of one of these genes, G7a (or BAT6), has been determined from cDNA and genomic clones. The single-copy G7a gene encodes a 1265-amino-acid protein of molecular mass 140,457 Da. Comparison of the derived amino acid sequence of the G7a protein with the National Biomedical Research Foundation protein databases revealed 42% identity in a 250-amino-acid overlap with Bacillus stearothermophilus valyl-tRNA synthetase, 38.0% identity in a 993-amino-acid overlap with Escherichia coli valyl-tRNA synthetase (val RS), and 48.3% identity in a 1043-amino-acid overlap with Saccharomyces cerevisiae valyl-tRNA synthetase. The protein sequence of G7a contains two short consensus sequences, His-Ile-Gly-His and Lys-Met-Ser-Lys-Ser, which is the typical signature structure of class I tRNA synthetases and indicative of the presence of the Rossman fold. In addition, the molecular mass of the G7a protein is the same as that of other mammalian valyl-tRNA synthetases. These features and the high sequence identity with yeast valyl-tRNA synthetase strongly support the fact that the G7a gene, located within the major histocompatibility complex, encodes the human valyl-tRNA synthetase.

scholarly journals β-Amino Acid Scan of a Class I Major Histocompatibility Complex-restricted Alloreactive T-cell Epitope

2001 ◽  
Vol 276 (27) ◽  
pp. 24525-24530 ◽  
Author(s):  
Stefan Reinelt ◽  
Merce Marti ◽  
Séverine Dédier ◽  
Thomas Reitinger ◽  
Gerd Folkers ◽  
...  
Keyword(s):  
Major Histocompatibility Complex ◽  
Amino Acid ◽  
T Cell ◽  
Cell Epitope ◽  
Class I ◽  
T Cell Epitope ◽  
Major Histocompatibility ◽  
Histocompatibility Complex ◽  
Alloreactive T Cell

scholarly journals Downregulation of Major Histocompatibility Complex Class I Molecules by Kaposi's Sarcoma-Associated Herpesvirus K3 and K5 Proteins

2000 ◽  
Vol 74 (11) ◽  
pp. 5300-5309 ◽  
Author(s):  
Satoshi Ishido ◽  
Chunyang Wang ◽  
Bok-Soo Lee ◽  
George B. Cohen ◽  
J. U. Jung
Keyword(s):  
Immune Response ◽  
Major Histocompatibility Complex ◽  
Amino Acid ◽  
Mhc Class I ◽  
Kaposi's Sarcoma ◽  
Kaposi’S Sarcoma ◽  
Class I ◽  
Major Histocompatibility ◽  
Histocompatibility Complex ◽  
Mhc Class I Molecules

ABSTRACT The T-cell-mediated immune response plays a central role in the defense against intracellular pathogens. To avoid this immune response, viruses have evolved elaborate mechanisms that target and modulate many different aspects of the host's immune system. A target common to many of these viruses is the major histocompatibility complex (MHC) class I molecules. Kaposi's sarcoma-associated herpesvirus (KSHV) encodes K3 and K5 zinc finger membrane proteins which remove MHC class I molecules from the cell surface. K3 and K5 exhibit 40% amino acid identity to each other and localize primarily near the plasma membrane. While K3 and K5 dramatically downregulated class I molecules, they displayed different specificities in downregulation of HLA allotypes. K5 significantly downregulated HLA-A and -B and downregulated HLA-C only weakly, but not HLA-E, whereas K3 downregulated all four HLA allotypes. This selective downregulation of HLA allotypes by K5 was partly due to differences in amino acid sequences in their transmembrane regions. Biochemical analyses demonstrated that while K3 and K5 did not affect expression and intracellular transport of class I molecules, their expression induced rapid endocytosis of the molecules. These results demonstrate that KSHV has evolved a novel immune evasion mechanism by harboring similar but distinct genes, K3 and K5, which target MHC class I molecules in different ways.

Sign in / Sign up

Export Citation Format

Share Document