PMID- 22122911
OWN - NLM
STAT- MEDLINE
DCOM- 20120222
LR  - 20211203
IS  - 1743-422X (Electronic)
IS  - 1743-422X (Linking)
VI  - 8
DP  - 2011 Nov 28
TI  - Sequence similarity between the erythrocyte binding domain of the Plasmodium 
      vivax Duffy binding protein and the V3 loop of HIV-1 strain MN reveals a 
      functional heparin binding motif involved in binding to the Duffy antigen 
      receptor for chemokines.
PG  - 523
LID - 10.1186/1743-422X-8-523 [doi]
AB  - BACKGROUND: The HIV surface glycoprotein gp120 (SU, gp120) and the Plasmodium 
      vivax Duffy binding protein (PvDBP) bind to chemokine receptors during infection 
      and have a site of amino acid sequence similarity in their binding domains that 
      often includes a heparin binding motif (HBM). Infection by either pathogen has 
      been found to be inhibited by polyanions. RESULTS: Specific polyanions that 
      inhibit HIV infection and bind to the V3 loop of X4 strains also inhibited 
      DBP-mediated infection of erythrocytes and DBP binding to the Duffy Antigen 
      Receptor for Chemokines (DARC). A peptide including the HBM of PvDBP had similar 
      affinity for heparin as RANTES and V3 loop peptides, and could be specifically 
      inhibited from heparin binding by the same polyanions that inhibit DBP binding to 
      DARC. However, some V3 peptides can competitively inhibit RANTES binding to 
      heparin, but not the PvDBP HBM peptide. Three other members of the DBP family 
      have an HBM sequence that is necessary for erythrocyte binding, however only the 
      protein which binds to DARC, the P. knowlesi alpha protein, is inhibited by 
      heparin from binding to erythrocytes. Heparitinase digestion does not affect the 
      binding of DBP to erythrocytes. CONCLUSION: The HBMs of DBPs that bind to DARC 
      have similar heparin binding affinities as some V3 loop peptides and chemokines, 
      are responsible for specific sulfated polysaccharide inhibition of parasite 
      binding and invasion of red blood cells, and are more likely to bind to negative 
      charges on the receptor than cell surface glycosaminoglycans.
FAU - Bolton, Michael J
AU  - Bolton MJ
AD  - Department of Microbiology and Immunology, Tulane University, 1430 Tulane Avenue, 
      New Orleans, LA 70112, USA.
FAU - Garry, Robert F
AU  - Garry RF
LA  - eng
GR  - RR018229/RR/NCRR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20111128
PL  - England
TA  - Virol J
JT  - Virology journal
JID - 101231645
RN  - 0 (ACKR1 protein, human)
RN  - 0 (Anti-HIV Agents)
RN  - 0 (Antigens, Protozoan)
RN  - 0 (Antimalarials)
RN  - 0 (Duffy Blood-Group System)
RN  - 0 (Duffy antigen binding protein, Plasmodium)
RN  - 0 (HIV Envelope Protein gp120)
RN  - 0 (Polyelectrolytes)
RN  - 0 (Polymers)
RN  - 0 (Protozoan Proteins)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (gp120 protein, Human immunodeficiency virus 1)
RN  - 0 (polyanions)
RN  - 9005-49-6 (Heparin)
SB  - IM
MH  - Amino Acid Sequence
MH  - Anti-HIV Agents/metabolism
MH  - Antigens, Protozoan/*genetics
MH  - Antimalarials/metabolism
MH  - Binding Sites
MH  - Duffy Blood-Group System/*metabolism
MH  - Erythrocytes/parasitology
MH  - HIV Envelope Protein gp120/*genetics
MH  - Heparin/metabolism
MH  - Humans
MH  - Molecular Sequence Data
MH  - Plasmodium knowlesi/*genetics/*pathogenicity
MH  - Plasmodium vivax/*genetics/*pathogenicity
MH  - Polyelectrolytes
MH  - Polymers/metabolism
MH  - Protein Binding
MH  - Protozoan Proteins/*genetics
MH  - Receptors, Cell Surface/*genetics/*metabolism
MH  - Sequence Homology, Amino Acid
PMC - PMC3240837
EDAT- 2011/11/30 06:00
MHDA- 2012/02/23 06:00
PMCR- 2011/11/28
CRDT- 2011/11/30 06:00
PHST- 2011/10/24 00:00 [received]
PHST- 2011/11/28 00:00 [accepted]
PHST- 2011/11/30 06:00 [entrez]
PHST- 2011/11/30 06:00 [pubmed]
PHST- 2012/02/23 06:00 [medline]
PHST- 2011/11/28 00:00 [pmc-release]
AID - 1743-422X-8-523 [pii]
AID - 10.1186/1743-422X-8-523 [doi]
PST - epublish
SO  - Virol J. 2011 Nov 28;8:523. doi: 10.1186/1743-422X-8-523.