TY - JOUR
T1 - Les protéines DING
T2 - Propriétés biochimiques, structurales, et capacité à inhiber la réplication du virus VIH-1
AU - Chabriere, Éric
AU - Elias, Mikael
AU - Hiblot, Julien
AU - Djeghader, Ahmed
AU - Schwartz, Christian
AU - Rohr, Olivier
AU - Masson, Patrick
PY - 2012/3
Y1 - 2012/3
N2 - DING proteins comprise an intriguing phosphate-binding protein family present in all animal phyla. Five different DING representatives have been described in humans. Euka-ryotic DING proteins are mostly involved in cellular processes such as cell cycle regulation, and also in pathological process such as rheumatoid arthritis and kidney stone formation. Although these proteins are ubiquitous in eukaryotes, no relevant locus or ORFhasyet been found in sequenced genomes. This lack of sequence information has considerably hampered functional and structural studies of these proteins, and has required the use of novel and original techniques such as ab initio protein sequencing based on a combination of X-ray crystallography and mass spectrometry. Sub-Angstrom structural resolution has elucidated the molecular binding mechanism of phosphate ions by these high-affinity proteins. Immu-nohistochemical studies show that these proteins are present in a wide variety of mouse tissues. Some DING proteins, particularly human phosphate binding protein (HPBP), can inhibit HIV replication. This inhibition takes place at the transcriptional step, which is not targeted by any current antiretroviral drug. Initial studies suggest that HPBP warrants animal testing. This recent discovery opens new possibilities for the treatment of HIV infection.
AB - DING proteins comprise an intriguing phosphate-binding protein family present in all animal phyla. Five different DING representatives have been described in humans. Euka-ryotic DING proteins are mostly involved in cellular processes such as cell cycle regulation, and also in pathological process such as rheumatoid arthritis and kidney stone formation. Although these proteins are ubiquitous in eukaryotes, no relevant locus or ORFhasyet been found in sequenced genomes. This lack of sequence information has considerably hampered functional and structural studies of these proteins, and has required the use of novel and original techniques such as ab initio protein sequencing based on a combination of X-ray crystallography and mass spectrometry. Sub-Angstrom structural resolution has elucidated the molecular binding mechanism of phosphate ions by these high-affinity proteins. Immu-nohistochemical studies show that these proteins are present in a wide variety of mouse tissues. Some DING proteins, particularly human phosphate binding protein (HPBP), can inhibit HIV replication. This inhibition takes place at the transcriptional step, which is not targeted by any current antiretroviral drug. Initial studies suggest that HPBP warrants animal testing. This recent discovery opens new possibilities for the treatment of HIV infection.
KW - HIV
KW - Phosphate-binding proteins
UR - http://www.scopus.com/inward/record.url?scp=84873942995&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84873942995&partnerID=8YFLogxK
U2 - 10.1016/s0001-4079(19)31806-0
DO - 10.1016/s0001-4079(19)31806-0
M3 - Article
C2 - 23472357
AN - SCOPUS:84873942995
SN - 0001-4079
VL - 196
SP - 693
EP - 704
JO - Bulletin de l'Academie Nationale de Medecine
JF - Bulletin de l'Academie Nationale de Medecine
IS - 3
ER -