Background: Common mental health problems are mainly treated in primary care settings and collaboration with mental health services is needed. Prior to re-organisation of the mental health care offer in a geographical area, a study was organized: 1) to evaluate GPs' opinions on their day-to-day practice with Patients with Mental Health Problems (PMHP) and on relationships with Mental Health Professionals (MHPro); 2) to identify factors associated with perceived need for collaboration with MHPro and with actual collaboration.

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Haloperidol was prescribed to a minority and targeted male patients hospitalized under constraint, using high dosages. Type and rate of co-prescriptions varied considerably between haloperidol and atypicals.

To identify HLA-DR-binding peptides within the human immunodeficiency virus (HIV)-1 proteins. 95 overlapping synthetic peptides representing the entire sequence of gp120-LAI were screened for their capacity to bind to two HLA-DR molecules with distant sequences (DR0401 and DR1101). By using a cell surface competitive binding assay, 56 DR-binding peptides were identified, of which 35 bound to both DR1101 and DR0401. A highly significant concordance was evidenced by statistical analysis between binding of peptides to one and to the other DR molecule, suggesting a high proportion of promiscuity among gp120 peptides, even though no clear sequence pattern accounting for such promiscuity was found. DR-binding peptides were located along the entire gp120 sequence. Yet, the majority of them (42 among 56) were concentrated in seven multiagretopic regions that were arbitrarily defined as regions containing four or more overlapping continuous peptides binding to DR1011 and/or DR0401. A good correlation was found between DR-binding regions or DR-binding peptides defined in this study and promiscuous T helper gp120 epitopes previously described in seropositive individuals. All these results suggest that the identification of multiagretopic DR-binding regions may be a great help for the predicition of protein determinants that have the likelihood of being promiscuous T helper epitopes in humans.

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To get further insight into the role of three polymorphic DR residues located in one alpha-helix of the HLA-DR binding groove, we studied how natural substitutions at positions 67, 71, and 86 on DR11 molecules influence MHC binding and/or T cell recognition of peptide HA306-320 and of monosubstituted peptide analogues. Our results show that: 1) Reactivities of all HA306-320-specific T cell clones tested are decreased by DR substitution at position 86 and can even be lowered by additional substitutions at position 71, and at positions 71 plus 67, indicating that these three residues are functionally important. 2) The functional effects of substitutions at positions 67, 71, and/or 86 cannot be explained by a decreased affinity of HA306-320 for the substituted DR11 molecules, as determined in binding assays. 3) More likely, they are explained by modifications of the conformation, orientation, or location of the peptide once bound in the HLA groove, because each individual DR substitution at positions 86, 71, and 67 differentially affects the binding ability of the same panel of 50 monosubstituted analogues. 4) This interpretation is reinforced by the identification of a small set of monosubstituted analogues that can compensate the functional effects of DR substitutions at positions 86, 86 plus 71, or 86 plus 71 plus 67, and thus restore T cell reactivities. All together these results strongly suggest that residues 67, 71, and 86 play a key role in interactions with HA306-320, probably by modifying the way the peptide is bound within the binding groove of HLA-DR11. Using the same DR11.1-restricted clones, we identified putative T cell and DR contact residues of HA306-320 by comparing DR binding and T cell-activating capacity of the peptide analogues. This analysis suggests that: 1) Residues 310, 311, 312, 313, and 316 are putative TCR contacts. 2) Peptide HA306-320 anchors to DR11.1 molecules mainly via residue Y-309, possibly at the vicinity of DR residue 86, whereas peptide residues 315 and 317 constitute minor aggregotopes that would be at the vicinity of DR residues 71 and/or 67. 3) Finally, residues 308, 310, and 314 might also be on the MHC side of the DR-peptide-TCR complex.