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R Benarous

Publications and source records attributed to R Benarous.

76 records · Page 5Linked to original sources
PubMedDate not supplied

Identification of a mouse cDNA fragment whose expressed polypeptide reacts with anti-recA antibodies.

We have previously reported the in vivo detection of a mouse nuclear protein that cross-reacts with antibodies raised against E coli recA protein. Here, we characterize monospecific anti-recA antibodies, their use for the immunological screening of a cDNA expression library and the isolation of a mouse cDNA fragment which codes for a polypeptide recognized by anti-recA antibodies. The cDNA fragment is 601 nucleotide long and was called KIN17(601). It contains an open reading frame coding for a 200 amino acid polypeptide. In kin17(200) polypeptide, there are amino acids identical to those that form one of the major antigenic determinants of recA protein. Kin17(200) polypeptide also displays a significant similarity with the helix 1 motif of several homeoproteins.

Amino Acid Sequence↗
PubMedDate not supplied

B-cell continuous epitopes of the SIVmac-251 envelope protein in experimentally infected macaques.

The humoral immune response of 34 macaques experimentally infected with SIVmac-251 was studied using a combination of an epitope library and synthetic peptides. The course of the immune response was checked for up to 9 months postinfection with a panel of clones expressing SIV fragments. A systematic study was performed with synthetic peptides covering the whole transmembrane (TM) and external (SU) envelope proteins. Seven major immunodominant epitopes were characterized. Four are localized in the SU protein: one in the V1 region (111-130), one in the Cys loop of the V3 region (311-330) and two in the C-terminal end (501-520 and 511-530). Three are localized in the TM protein: one in the extracellular domain (601-619), one in the anchor domain (731-750) and one in the intracytoplasmic domain (861-881). Among these epitopes, only one, 601-619, was found to be reactive with all sera and can be defined as the principal immunodominant epitope.

Amino Acid Sequence↗
PubMedDate not supplied

Inhibition of prokaryotic cell growth by HIV1 Vpr.

We have cloned the nef, vif, vpr and vpu genes of HIV1 in the pGEX system to produce auxiliary proteins of HIV1 as N-terminal fusions with glutathione S-transferase (GST). Some GST proteins are difficult to obtain under standard conditions. The synthesis and solubility varied considerably from one protein to another. We investigated the reasons for the poor production of GST-Vpr, GST-Vpu and GST-Vif. Interestingly, using this GST prokaryotic model, we demonstrated that Vpr, which is known to block the cell cycle of mammalian and yeast cells at the G2 phase, is also bacteriostatic for Escherichia coli. The effect on E. coli was specific to Vpr, and was not linked to the expression of the other HIV1 proteins. This suggests that Vpr interferes with components of cell replication that are conserved from prokaryotes to eukaryotes. Thus, E. coli appears to be a convenient model system for studies on the function of Vpr.

Cell Division↗