Patterns of reticulate evolution for the classical class I and II HLA loci

1998 ◽  
Vol 48 (5) ◽  
pp. 312-323 ◽  
Author(s):  
I. B. Jakobsen ◽  
Susan R. Wilson ◽  
S. Easteal
2019 ◽  
Vol 71 (10) ◽  
pp. 647-663 ◽  
Author(s):  
Nicola D. Potts ◽  
Coraline Bichet ◽  
Laurence Merat ◽  
Edouard Guitton ◽  
Andrew P. Krupa ◽  
...  

2007 ◽  
Vol 178 (9) ◽  
pp. 5744-5752 ◽  
Author(s):  
Iain Shaw ◽  
Timothy J. Powell ◽  
Denise A. Marston ◽  
Ken Baker ◽  
Andrew van Hateren ◽  
...  
Keyword(s):  
Class I ◽  

2001 ◽  
Vol 53 (6) ◽  
pp. 490-500 ◽  
Author(s):  
Christine Renard ◽  
Marcel Vaiman ◽  
Nuchanard Chiannilkulchai ◽  
Laurence Cattolico ◽  
Catherine Robert ◽  
...  

1999 ◽  
Vol 49 (6) ◽  
pp. 479-490 ◽  
Author(s):  
Benny P. Shum ◽  
R. Rajalingam ◽  
Katharine E. Magor ◽  
K. Azumi ◽  
William H. Carr ◽  
...  
Keyword(s):  
Class I ◽  

Author(s):  
C. Bordallo ◽  
W. I. Frels ◽  
J. Lunney ◽  
A. Rosenberg ◽  
S. Rudikoff ◽  
...  

2010 ◽  
Vol 207 (9) ◽  
pp. 2033-2041 ◽  
Author(s):  
Boyoun Park ◽  
Eric Spooner ◽  
Brandy L. Houser ◽  
Jack L. Strominger ◽  
Hidde L. Ploegh

Human cytomegalovirus (HCMV) encodes an endoplasmic reticulum (ER)-resident transmembrane glycoprotein, US10, expressed early in the replicative cycle of HCMV as part of the same cluster that encodes the known immunoevasins US2, US3, US6, and US11. We show that US10 down-regulates cell surface expression of HLA-G, but not that of classical class I MHC molecules. The unique and short cytoplasmic tail of HLA-G (RKKSSD) is essential in its role as a US10 substrate, and a tri-leucine motif in the cytoplasmic tail of US10 is responsible for down-regulation of HLA-G. Both the kinetics of HLA-G degradation and the mechanisms responsible appear to be distinct from those used by the US2 and US11 pathways, suggesting the existence of a third route of protein dislocation from the ER. We show that US10-mediated degradation of HLA-G interferes with HLA-G–mediated NK cell inhibition. Given the role of HLA-G in protecting the fetus from attack by the maternal immune system and in directing the differentiation of human dendritic cells to promote the evolution of regulatory T cells, HCMV likely targets the HLA-G–dependent axis of immune recognition no less efficiently than it interferes with classical class I MHC–restricted antigen presentation.


Cells ◽  
2019 ◽  
Vol 8 (9) ◽  
pp. 978 ◽  
Author(s):  
Shiina ◽  
Blancher

Among the non-human primates used in experimental medicine, cynomolgus macaques (Macaca fascicularis hereafter referred to as Mafa) are increasingly selected for the ease with which they are maintained and bred in captivity. Macaques belong to Old World monkeys and are phylogenetically much closer to humans than rodents, which are still the most frequently used animal model. Our understanding of the Mafa genome has progressed rapidly in recent years and has greatly benefited from the latest technical advances in molecular genetics. Cynomolgus macaques are widespread in Southeast Asia and numerous studies have shown a distinct genetic differentiation of continental and island populations. The major histocompatibility complex of cynomolgus macaque (Mafa MHC) is organized in the same way as that of human, but it differs from the latter by its high degree of classical class I gene duplication. Human polymorphic MHC regions play a pivotal role in allograft transplantation and have been associated with more than 100 diseases and/or phenotypes. The Mafa MHC polymorphism similarly plays a crucial role in experimental allografts of organs and stem cells. Experimental results show that the Mafa MHC class I and II regions influence the ability to mount an immune response against infectious pathogens and vaccines. MHC also affects cynomolgus macaque reproduction and impacts on numerous biological parameters. This review describes the Mafa MHC polymorphism and the methods currently used to characterize it. We discuss some of the major areas of experimental medicine where an effect induced by MHC polymorphism has been demonstrated.


1991 ◽  
Vol 32 ◽  
pp. 82
Author(s):  
Z. Liu ◽  
M.A. Fernandez-Viña ◽  
J.R. Moraes ◽  
Y. Luo ◽  
P. Stastny

1989 ◽  
Vol 170 (3) ◽  
pp. 777-795 ◽  
Author(s):  
A M Livingstone ◽  
S J Powis ◽  
A G Diamond ◽  
G W Butcher ◽  
J C Howard

The RT1.A locus of the rat MHC encodes the H chain of the single classical class I molecule of this species. One of the alleles of this polymorphic locus, RT1.Aa, is present in several laboratory inbred, congenic, and MHC recombinant rat strains. Studies of the RT1.Aa class I molecule from a number of these strains as a target for CTL show that its antigenicity, both as an alloantigen and a restricting element, is subject to gain and loss alterations by the action of a gene mapping in the MHC to the right of RT1.A. This locus is apparently present in two allelic forms (one possibly a null allele) corresponding to the presence or absence of a dominant transacting modifier, and has been named class I modification, or cim. The antigenic change brought about by cim is scarcely detectable serologically but highly immunogenic for CTL. Biochemical investigations show that cim affects the post-translational modification of RT1.Aa.


2014 ◽  
Vol 2014 ◽  
pp. 1-15 ◽  
Author(s):  
Erick C. Castelli ◽  
Luciana C. Veiga-Castelli ◽  
Layale Yaghi ◽  
Philippe Moreau ◽  
Eduardo A. Donadi

HLA-Ghas a relevant role in immune response regulation. The overall structure of theHLA-Gcoding region has been maintained during the evolution process, in which most of its variable sites are synonymous mutations or coincide with introns, preserving major functionalHLA-Gproperties. TheHLA-Gpromoter region is different from the classical class I promoters, mainly because (i) it lacks regulatory responsive elements for IFN-γand NF-κB, (ii) the proximal promoter region (within 200 bases from the first translated ATG) does not mediate transactivation by the principal HLA class I transactivation mechanisms, and (iii) the presence of identified alternative regulatory elements (heat shock, progesterone and hypoxia-responsive elements) and unidentified responsive elements for IL-10, glucocorticoids, and other transcription factors is evident. At least three variable sites in the 3′ untranslated region have been studied that may influenceHLA-Gexpression by modifying mRNA stability or microRNA binding sites, including the 14-base pair insertion/deletion, +3142C/G and +3187A/G polymorphisms. Other polymorphic sites have been described, but there are no functional studies on them. TheHLA-Gcoding region polymorphisms might influence isoform production and at least two null alleles with premature stop codons have been described. We reviewed the structure of theHLA-Gpromoter region and its implication in transcriptional gene control, the structure of theHLA-G3′UTR and the major actors of the posttranscriptional gene control, and, finally, the presence of regulatory elements in the coding region.


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