HLA-G: Difference between revisions
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{{ | '''HLA-G histocompatibility antigen, class I, G''', also known as human leukocyte antigen G ('''HLA-G'''), is a [[protein]] that in humans is encoded by the ''HLA-G'' [[gene]].<ref name= "entrez"/> | ||
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| | HLA-G belongs to the [[human leukocyte antigen|HLA]] nonclassical class I heavy chain paralogues. This class I molecule is a heterodimer consisting of a heavy chain and a light chain ([[beta-2 microglobulin]]). The heavy chain is anchored in the membrane. HLA-G is expressed on fetal derived placental cells. The heavy chain is approximately 45 kDa and its gene contains 8 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the alpha1 and alpha2 domain, which both bind the peptide, exon 4 encodes the alpha3 domain, exon 5 encodes the transmembrane region, and exon 6 encodes the cytoplasmic tail.<ref name= "entrez">{{cite web | title = Entrez Gene: HLA-G HLA-G histocompatibility antigen, class I, G| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3135| accessdate = }}</ref> Exon 7 and 8 are not translated due to a stop codon present in exon 6.<ref>{{Cite journal|last=Castelli|first=Erick C.|last2=Mendes-Junior|first2=Celso T.|last3=Veiga-Castelli|first3=Luciana C.|last4=Roger|first4=Michel|last5=Moreau|first5=Philippe|last6=Donadi|first6=Eduardo A.|date=2011-11-01|title=A Comprehensive Study of Polymorphic Sites along the HLA-G Gene: Implication for Gene Regulation and Evolution|url=http://mbe.oxfordjournals.org/content/28/11/3069|journal=Molecular Biology and Evolution|language=en|volume=28|issue=11|pages=3069–3086|doi=10.1093/molbev/msr138|issn=0737-4038|pmid=21622995}}</ref> | ||
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| | == Function == | ||
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}} | HLA-G may play a role in [[immune tolerance in pregnancy]], being expressed in the [[placenta]] by extravillous trophoblast cells (EVT), while the classical [[MHC class I]] genes ([[HLA-A]] and [[HLA-B]]) are not.<ref name="isbn0-7216-0004-2">{{cite book |author1=Jay Iams |author2=Creasy, Robert K. |author3=Resnik, Robert |author4=Robert Reznik | title = Maternal-fetal medicine | edition = | language = | publisher = W.B. Saunders Co | location = Philadelphia | year = 2004 | origyear = | pages = 31–32 | quote = | isbn = 0-7216-0004-2 | oclc = | doi = | url = | accessdate = }}</ref> As HLA-G was first identified in placenta samples, many studies have evaluated its role in pregnancy disorders, such as preeclampsia and recurrent pregnancy loss.<ref>{{Cite journal|last=Michita|first=Rafael Tomoya|last2=Zambra|first2=Francis Maria Báo|last3=Fraga|first3=Lucas Rosa|last4=Sanseverino|first4=Maria Teresa Vieira|last5=Callegari-Jacques|first5=Sidia Maria|last6=Vianna|first6=Priscila|last7=Chies|first7=José Artur Bogo|title=A tug-of-war between tolerance and rejection – New evidence for 3′UTR HLA-G haplotypes influence in recurrent pregnancy loss|url=http://linkinghub.elsevier.com/retrieve/pii/S0198885916301574|journal=Human Immunology|volume=77|issue=10|pages=892–897|doi=10.1016/j.humimm.2016.07.004}}</ref> its downregulation is related to HLA-A and -B downregulation results in protection from [[cytotoxic T cell]] responses, but would in theory result in a ''missing self'' response by [[natural killer cell]]s. HLA-G is a ligand for NK cell inhibitory receptor [[KIR2DL4]], and therefore expression of this HLA by the trophoblast defends it against NK cell-mediated death.<ref name="pmid20061017">{{cite journal |author=Lash, G, Robson, S, Bulmer, J. |title=Review: Functional role of uterine natural killer (uNK) cells in human early pregnancy decidua |journal=Placenta |volume=31 |issue=S |pages=87–92 |year=2010 |pmid=20061017 |doi=10.1016/j.placenta.2009.12.022}}</ref> | ||
However, a large family with several members bearing only "null" HLA-G alleles has been found. None of these homozygous subjects have pregnancy or birth difficulties; nor do they present immunodeficiencies, autoimmune diseases, or tumors.<ref name="pmid9089111">{{cite journal |vauthors=Suárez MB, Morales P, Castro MJ, Fernández V, Varela P, Alvarez M, Martínez-Laso J, Arnaiz-Villena A | title = A new HLA-G allele (HLA-G*0105N) and its distribution in the Spanish population | journal = Immunogenetics | volume = 45 | issue = 6 | pages = 464–5 | year = 1997 | pmid = 9089111 | doi = 10.1007/s002510050235}}</ref><ref name="pmid11034559">{{cite journal |vauthors=Casro MJ, Morales P, Rojo-Amigo R, Martinez-Laso J, Allende L, Varela P, Garcia-Berciano M, Guillen-Perales J, Arnaiz-Villena A | title = Homozygous HLA-G*0105N healthy individuals indicate that membrane-anchored HLA-G1 molecule is not necessary for survival | journal = Tissue Antigens | volume = 56 | issue = 3 | pages = 232–9 |date=September 2000 | pmid = 11034559 | doi = 10.1034/j.1399-0039.2000.560305.x}}</ref> It is striking that this "null" allele (HLA-G*01:05N), while it is quite frequent in some populations, like in Iranians, it is almost absent in some Amerindian populations.<ref name="pmid23261410">{{cite journal |vauthors=Arnaiz-Villena A, Enriquez-de-Salamanca M, Areces C, Alonso-Rubio J, Abd-El-Fatah-Khalil S, Fernandez-Honrado M, Rey D | title = HLA-G(∗)01:05N null allele in Mayans (Guatemala) and Uros (Titikaka Lake, Peru): Evolution and population genetics | journal = Hum. Immunol. | volume = 74 | issue = 4 | pages = 478–82 |date=April 2013 | pmid = 23261410 | doi = 10.1016/j.humimm.2012.12.013 }}</ref> Also, some higher primates do not show all MHC-G isoforms.<ref name="pmid11137222">{{cite journal |vauthors=Castro MJ, Morales P, Martinez-Laso J, Allende L, Rojo-Amigo R, Gonzalez-Hevilla M, Varela P, Moscoso J, Garcia-Berciano M, Arnaiz-Villena A | title = Lack of MHC-G4 and soluble (G5, G6) isoforms in the higher primates, Pongidae | journal = Hum. Immunol. | volume = 61 | issue = 11 | pages = 1164–8 |date=November 2000 | pmid = 11137222 | doi = 10.1016/s0198-8859(00)00189-0}}</ref> In addition, Cercopithecinae middle-sized Old World monkeys do not bear full MHC-G molecules since all of these monkeys present stop codons at MHC-G DNA.<ref name="pmid8606053">{{cite journal |vauthors=Castro MJ, Morales P, Fernández-Soria V, Suarez B, Recio MJ, Alvarez M, Martín-Villa M, Arnaiz-Villena A | title = Allelic diversity at the primate Mhc-G locus: exon 3 bears stop codons in all Cercopithecinae sequences | journal = Immunogenetics | volume = 43 | issue = 6 | pages = 327–36 | year = 1996 | pmid = 8606053 | doi = 10.1007/bf02199801 }}</ref> All of these anomalies must be studied. | |||
The presence of soluble HLA-G (sHLA-G) in embryos is associated with better [[pregnancy rate]]s. In order to optimize pregnancy rates, there is significant evidence that a morphological scoring system is the best strategy for the selection of embryos.<ref name=Rebmann>{{cite journal |vauthors=Rebmann V, Switala M, Eue I, Grosse-Wilde H |title=Soluble HLA-G is an independent factor for the prediction of pregnancy outcome after ART: a German multi-centre study |journal=Hum Reprod |volume= 25|issue= 7|pages= 1691–8|date=May 2010 |pmid=20488801 |doi=10.1093/humrep/deq120 |url=}}</ref> However, presence of soluble HLA-G might be considered as a second parameter if a choice has to be made between embryos of morphologically equal quality.<ref name=Rebmann/> | |||
==Interactions== | |||
{{ | HLA-G has been shown to [[Protein-protein interaction|interact]] with [[CD8A]].<ref name="pmid10809759">{{cite journal |vauthors=Gao GF, Willcox BE, Wyer JR, Boulter JM, O'Callaghan CA, Maenaka K, Stuart DI, Jones EY, Van Der Merwe PA, Bell JI, Jakobsen BK | title = Classical and nonclassical class I major histocompatibility complex molecules exhibit subtle conformational differences that affect binding to CD8alphaalpha | journal = J. Biol. Chem. | volume = 275 | issue = 20 | pages = 15232–8 |date=May 2000 | pmid = 10809759 | doi = 10.1074/jbc.275.20.15232| url = }}</ref><ref name="pmid1908512">{{cite journal |vauthors=Sanders SK, Giblin PA, Kavathas P | title = Cell-cell adhesion mediated by CD8 and human histocompatibility leukocyte antigen G, a nonclassical major histocompatibility complex class 1 molecule on cytotrophoblasts | journal = J. Exp. Med. | volume = 174 | issue = 3 | pages = 737–40 |date=September 1991 | pmid = 1908512 | pmc = 2118947 | doi = 10.1084/jem.174.3.737| url = }}</ref> | ||
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==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
*{{cite journal |vauthors=Carosella ED, Favier B, Rouas-Freiss N, Moreau P, LeMaoult J |title=Beyond the increasing complexity of the immunomodulatory HLA-G molecule |journal=Blood |volume=111 |issue= 10 |pages= 4862–70 |year= 2008 |pmid= 18334671 |doi=10.1182/blood-2007-12-127662 }} | |||
*{{cite journal |vauthors=Carosella ED, Moreau P, LeMaoult J, Rouas-Freiss N |title=HLA-G: From biology to clinical benefits |journal=Trends in Immunology |volume=29 |issue= 3|pages= 125–32 |year= 2008 |pmid= 18249584 |doi=10.1016/j.it.2007.11.005 }} | |||
*{{cite journal | | {{PBB_Further_reading | citations = | ||
*{{cite journal | | *{{cite journal | author=Arnaiz-Villena A |title=Primate Mhc-E and -G alleles |journal=Immunogenetics |volume=46 |issue= 4 |pages= 251–66 |year= 1997 |pmid= 9218527 |doi=10.1007/s002510050271 |name-list-format=vanc| author2=Martinez-Laso J | author3=Alvarez M | display-authors=3 | last4=Castro | first4=Maria J. | last5=Varela | first5=Pilar | last6=Gomez-Casado | first6=Eduardo | last7=Suarez | first7=Belen | last8=Recio | first8=María José | last9=Vargas-Alarcón | first9=Gilberto }} | ||
*{{cite journal | author= | *{{cite journal | author=Le Bouteiller P |title=HLA-G in the human placenta: expression and potential functions |journal=Biochem. Soc. Trans. |volume=28 |issue= 2 |pages= 208–12 |year= 2000 |pmid= 10816129 |doi= }} | ||
*{{cite journal |vauthors=Geyer M, Fackler OT, Peterlin BM |title=Structure–function relationships in HIV-1 Nef |journal=EMBO Rep. |volume=2 |issue= 7 |pages= 580–5 |year= 2001 |pmid= 11463741 |doi= 10.1093/embo-reports/kve141 | pmc=1083955 }} | |||
*{{cite journal | author= | *{{cite journal |vauthors=Langat DK, Hunt JS |title=Do nonhuman primates comprise appropriate experimental models for studying the function of human leukocyte antigen-G? |journal=Biol. Reprod. |volume=67 |issue= 5 |pages= 1367–74 |year= 2003 |pmid= 12390864 |doi=10.1095/biolreprod.102.005587 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Moreau P, Dausset J, Carosella ED, Rouas-Freiss N |title=Viewpoint on the functionality of the human leukocyte antigen-G null allele at the fetal-maternal interface |journal=Biol. Reprod. |volume=67 |issue= 5 |pages= 1375–8 |year= 2003 |pmid= 12390865 |doi=10.1095/biolreprod.102.005439 }} | ||
*{{cite journal | | *{{cite journal | author=Moreau P |title=HLA-G protein processing and transport to the cell surface |journal=Cell. Mol. Life Sci. |volume=59 |issue= 9 |pages= 1460–6 |year= 2002 |pmid= 12440768 |doi=10.1007/s00018-002-8521-8 |name-list-format=vanc| author2=Rousseau P | author3=Rouas-Freiss N | display-authors=3 | last4=Le Discorde | first4=M. | last5=Dausset | first5=J. | last6=Carosella | first6=E. D. }} | ||
*{{cite journal | | *{{cite journal | author=Greenway AL |title=HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication |journal=J. Biosci. |volume=28 |issue= 3 |pages= 323–35 |year= 2004 |pmid= 12734410 |doi=10.1007/BF02970151 |name-list-format=vanc| author2=Holloway G | author3=McPhee DA | display-authors=3 | last4=Ellis | first4=Phoebe | last5=Cornall | first5=Alyssa | last6=Lidman | first6=Michael }} | ||
*{{cite journal | author= | *{{cite journal |vauthors=Bénichou S, Benmerah A |title=[The HIV nef and the Kaposi-sarcoma-associated virus K3/K5 proteins: "parasites"of the endocytosis pathway] |journal=Med Sci (Paris) |volume=19 |issue= 1 |pages= 100–6 |year= 2003 |pmid= 12836198 |doi= 10.1051/medsci/2003191100}} | ||
*{{cite journal |vauthors=Le Bouteiller P, Legrand-Abravanel F, Solier C |title=Soluble HLA-G1 at the materno-foetal interface--a review |journal=Placenta |volume=24 Suppl A |issue= |pages= S10–5 |year= 2004 |pmid= 12842408 |doi=10.1053/plac.2002.0931 }} | |||
*{{cite journal | author= | *{{cite journal |vauthors=Sköld M, Behar SM |title=Role of CD1d-Restricted NKT Cells in Microbial Immunity |journal=Infect. Immun. |volume=71 |issue= 10 |pages= 5447–55 |year= 2003 |pmid= 14500461 |doi=10.1128/IAI.71.10.5447-5455.2003 | pmc=201095 }} | ||
*{{cite journal |vauthors=Wiendl H, Mitsdoerffer M, Weller M |title=Express and protect yourself: the potential role of HLA-G on muscle cells and in inflammatory myopathies |journal=Hum. Immunol. |volume=64 |issue= 11 |pages= 1050–6 |year= 2004 |pmid= 14602235 |doi=10.1016/j.humimm.2003.07.001 }} | |||
*{{cite journal | | *{{cite journal |vauthors=Urosevic M, Dummer R |title=HLA-G in skin cancer: a wolf in sheep's clothing? |journal=Hum. Immunol. |volume=64 |issue= 11 |pages= 1073–80 |year= 2004 |pmid= 14602238 |doi=10.1016/j.humimm.2003.08.351 }} | ||
*{{cite journal | | *{{cite journal | author=Carosella ED |title=HLA-G molecules: from maternal-fetal tolerance to tissue acceptance |journal=Adv. Immunol. |volume=81 |issue= |pages= 199–252 |year= 2004 |pmid= 14711057 |doi=10.1016/S0065-2776(03)81006-4 |name-list-format=vanc| author2=Moreau P | author3=Le Maoult J | display-authors=3 | series=Advances in Immunology | last4=Lediscorde | first4=M | last5=Dausset | first5=J | last6=Rouasfreiss | first6=N | isbn=978-0-12-022481-4 }} | ||
*{{cite journal | | *{{cite journal | author=Leavitt SA |title=Interactions of HIV-1 proteins gp120 and Nef with cellular partners define a novel allosteric paradigm |journal=Curr. Protein Pept. Sci. |volume=5 |issue= 1 |pages= 1–8 |year= 2004 |pmid= 14965316 |doi=10.2174/1389203043486955 |name-list-format=vanc| author2=SchOn A | author3=Klein JC | display-authors=3 | last4=Manjappara | first4=Uma | last5=m. Chaiken | first5=Irwin | last6=Freire | first6=Ernesto }} | ||
*{{cite journal | | *{{cite journal | author=Le Maoult J |title=[HLA-G in organ transplantation] |journal=Pathol. Biol. |volume=52 |issue= 2 |pages= 97–103 |year= 2004 |pmid= 15001239 |doi= 10.1016/j.patbio.2003.04.006 |name-list-format=vanc| author2=Rouas-Freiss N | author3=Le Discorde M | display-authors=3 | last4=Moreau | first4=P | last5=Carosella | first5=ED }} | ||
*{{cite journal | | *{{cite journal | author=Tolstrup M |title=HIV/SIV escape from immune surveillance: focus on Nef |journal=Curr. HIV Res. |volume=2 |issue= 2 |pages= 141–51 |year= 2004 |pmid= 15078178 |doi=10.2174/1570162043484924 |name-list-format=vanc| author2=Ostergaard L | author3=Laursen AL | display-authors=3 | last4=Pedersen | first4=Skou F. | last5=Duch | first5=Mogens }} | ||
*{{cite journal | | *{{cite journal |vauthors=Joseph AM, Kumar M, Mitra D |title=Nef: "necessary and enforcing factor" in HIV infection |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 87–94 |year= 2005 |pmid= 15638726 |doi=10.2174/1570162052773013 }} | ||
*{{cite journal | | *{{cite journal |vauthors=McIntire RH, Hunt JS |title=Antigen presenting cells and HLA-G--a review |journal=Placenta |volume=26 Suppl A |issue= |pages= S104–9 |year= 2005 |pmid= 15837058 |doi= 10.1016/j.placenta.2005.01.006 }} | ||
*{{cite journal |vauthors=Anderson JL, Hope TJ |title=HIV accessory proteins and surviving the host cell |journal=Current HIV/AIDS reports |volume=1 |issue= 1 |pages= 47–53 |year= 2005 |pmid= 16091223 |doi=10.1007/s11904-004-0007-x }} | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
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HLA-G histocompatibility antigen, class I, G, also known as human leukocyte antigen G (HLA-G), is a protein that in humans is encoded by the HLA-G gene.[1]
HLA-G belongs to the HLA nonclassical class I heavy chain paralogues. This class I molecule is a heterodimer consisting of a heavy chain and a light chain (beta-2 microglobulin). The heavy chain is anchored in the membrane. HLA-G is expressed on fetal derived placental cells. The heavy chain is approximately 45 kDa and its gene contains 8 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the alpha1 and alpha2 domain, which both bind the peptide, exon 4 encodes the alpha3 domain, exon 5 encodes the transmembrane region, and exon 6 encodes the cytoplasmic tail.[1] Exon 7 and 8 are not translated due to a stop codon present in exon 6.[2]
Function
HLA-G may play a role in immune tolerance in pregnancy, being expressed in the placenta by extravillous trophoblast cells (EVT), while the classical MHC class I genes (HLA-A and HLA-B) are not.[3] As HLA-G was first identified in placenta samples, many studies have evaluated its role in pregnancy disorders, such as preeclampsia and recurrent pregnancy loss.[4] its downregulation is related to HLA-A and -B downregulation results in protection from cytotoxic T cell responses, but would in theory result in a missing self response by natural killer cells. HLA-G is a ligand for NK cell inhibitory receptor KIR2DL4, and therefore expression of this HLA by the trophoblast defends it against NK cell-mediated death.[5]
However, a large family with several members bearing only "null" HLA-G alleles has been found. None of these homozygous subjects have pregnancy or birth difficulties; nor do they present immunodeficiencies, autoimmune diseases, or tumors.[6][7] It is striking that this "null" allele (HLA-G*01:05N), while it is quite frequent in some populations, like in Iranians, it is almost absent in some Amerindian populations.[8] Also, some higher primates do not show all MHC-G isoforms.[9] In addition, Cercopithecinae middle-sized Old World monkeys do not bear full MHC-G molecules since all of these monkeys present stop codons at MHC-G DNA.[10] All of these anomalies must be studied.
The presence of soluble HLA-G (sHLA-G) in embryos is associated with better pregnancy rates. In order to optimize pregnancy rates, there is significant evidence that a morphological scoring system is the best strategy for the selection of embryos.[11] However, presence of soluble HLA-G might be considered as a second parameter if a choice has to be made between embryos of morphologically equal quality.[11]
Interactions
HLA-G has been shown to interact with CD8A.[12][13]
References
- ↑ 1.0 1.1 "Entrez Gene: HLA-G HLA-G histocompatibility antigen, class I, G".
- ↑ Castelli, Erick C.; Mendes-Junior, Celso T.; Veiga-Castelli, Luciana C.; Roger, Michel; Moreau, Philippe; Donadi, Eduardo A. (2011-11-01). "A Comprehensive Study of Polymorphic Sites along the HLA-G Gene: Implication for Gene Regulation and Evolution". Molecular Biology and Evolution. 28 (11): 3069–3086. doi:10.1093/molbev/msr138. ISSN 0737-4038. PMID 21622995.
- ↑ Jay Iams; Creasy, Robert K.; Resnik, Robert; Robert Reznik (2004). Maternal-fetal medicine. Philadelphia: W.B. Saunders Co. pp. 31–32. ISBN 0-7216-0004-2.
- ↑ Michita, Rafael Tomoya; Zambra, Francis Maria Báo; Fraga, Lucas Rosa; Sanseverino, Maria Teresa Vieira; Callegari-Jacques, Sidia Maria; Vianna, Priscila; Chies, José Artur Bogo. "A tug-of-war between tolerance and rejection – New evidence for 3′UTR HLA-G haplotypes influence in recurrent pregnancy loss". Human Immunology. 77 (10): 892–897. doi:10.1016/j.humimm.2016.07.004.
- ↑ Lash, G, Robson, S, Bulmer, J. (2010). "Review: Functional role of uterine natural killer (uNK) cells in human early pregnancy decidua". Placenta. 31 (S): 87–92. doi:10.1016/j.placenta.2009.12.022. PMID 20061017.
- ↑ Suárez MB, Morales P, Castro MJ, Fernández V, Varela P, Alvarez M, Martínez-Laso J, Arnaiz-Villena A (1997). "A new HLA-G allele (HLA-G*0105N) and its distribution in the Spanish population". Immunogenetics. 45 (6): 464–5. doi:10.1007/s002510050235. PMID 9089111.
- ↑ Casro MJ, Morales P, Rojo-Amigo R, Martinez-Laso J, Allende L, Varela P, Garcia-Berciano M, Guillen-Perales J, Arnaiz-Villena A (September 2000). "Homozygous HLA-G*0105N healthy individuals indicate that membrane-anchored HLA-G1 molecule is not necessary for survival". Tissue Antigens. 56 (3): 232–9. doi:10.1034/j.1399-0039.2000.560305.x. PMID 11034559.
- ↑ Arnaiz-Villena A, Enriquez-de-Salamanca M, Areces C, Alonso-Rubio J, Abd-El-Fatah-Khalil S, Fernandez-Honrado M, Rey D (April 2013). "HLA-G(∗)01:05N null allele in Mayans (Guatemala) and Uros (Titikaka Lake, Peru): Evolution and population genetics". Hum. Immunol. 74 (4): 478–82. doi:10.1016/j.humimm.2012.12.013. PMID 23261410.
- ↑ Castro MJ, Morales P, Martinez-Laso J, Allende L, Rojo-Amigo R, Gonzalez-Hevilla M, Varela P, Moscoso J, Garcia-Berciano M, Arnaiz-Villena A (November 2000). "Lack of MHC-G4 and soluble (G5, G6) isoforms in the higher primates, Pongidae". Hum. Immunol. 61 (11): 1164–8. doi:10.1016/s0198-8859(00)00189-0. PMID 11137222.
- ↑ Castro MJ, Morales P, Fernández-Soria V, Suarez B, Recio MJ, Alvarez M, Martín-Villa M, Arnaiz-Villena A (1996). "Allelic diversity at the primate Mhc-G locus: exon 3 bears stop codons in all Cercopithecinae sequences". Immunogenetics. 43 (6): 327–36. doi:10.1007/bf02199801. PMID 8606053.
- ↑ 11.0 11.1 Rebmann V, Switala M, Eue I, Grosse-Wilde H (May 2010). "Soluble HLA-G is an independent factor for the prediction of pregnancy outcome after ART: a German multi-centre study". Hum Reprod. 25 (7): 1691–8. doi:10.1093/humrep/deq120. PMID 20488801.
- ↑ Gao GF, Willcox BE, Wyer JR, Boulter JM, O'Callaghan CA, Maenaka K, Stuart DI, Jones EY, Van Der Merwe PA, Bell JI, Jakobsen BK (May 2000). "Classical and nonclassical class I major histocompatibility complex molecules exhibit subtle conformational differences that affect binding to CD8alphaalpha". J. Biol. Chem. 275 (20): 15232–8. doi:10.1074/jbc.275.20.15232. PMID 10809759.
- ↑ Sanders SK, Giblin PA, Kavathas P (September 1991). "Cell-cell adhesion mediated by CD8 and human histocompatibility leukocyte antigen G, a nonclassical major histocompatibility complex class 1 molecule on cytotrophoblasts". J. Exp. Med. 174 (3): 737–40. doi:10.1084/jem.174.3.737. PMC 2118947. PMID 1908512.
Further reading
- Carosella ED, Favier B, Rouas-Freiss N, Moreau P, LeMaoult J (2008). "Beyond the increasing complexity of the immunomodulatory HLA-G molecule". Blood. 111 (10): 4862–70. doi:10.1182/blood-2007-12-127662. PMID 18334671.
- Carosella ED, Moreau P, LeMaoult J, Rouas-Freiss N (2008). "HLA-G: From biology to clinical benefits". Trends in Immunology. 29 (3): 125–32. doi:10.1016/j.it.2007.11.005. PMID 18249584.
- Arnaiz-Villena A, Martinez-Laso J, Alvarez M, et al. (1997). "Primate Mhc-E and -G alleles". Immunogenetics. 46 (4): 251–66. doi:10.1007/s002510050271. PMID 9218527.
- Le Bouteiller P (2000). "HLA-G in the human placenta: expression and potential functions". Biochem. Soc. Trans. 28 (2): 208–12. PMID 10816129.
- Geyer M, Fackler OT, Peterlin BM (2001). "Structure–function relationships in HIV-1 Nef". EMBO Rep. 2 (7): 580–5. doi:10.1093/embo-reports/kve141. PMC 1083955. PMID 11463741.
- Langat DK, Hunt JS (2003). "Do nonhuman primates comprise appropriate experimental models for studying the function of human leukocyte antigen-G?". Biol. Reprod. 67 (5): 1367–74. doi:10.1095/biolreprod.102.005587. PMID 12390864.
- Moreau P, Dausset J, Carosella ED, Rouas-Freiss N (2003). "Viewpoint on the functionality of the human leukocyte antigen-G null allele at the fetal-maternal interface". Biol. Reprod. 67 (5): 1375–8. doi:10.1095/biolreprod.102.005439. PMID 12390865.
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