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2.
Ann Readapt Med Phys ; 46(8): 525-38, 2003 Nov.
Article in French | MEDLINE | ID: mdl-14585530

ABSTRACT

OBJECTIVE: To explore the impact of the brain injury of a parent on his child's behavioural and emotional symptoms and personal experience. PATIENTS AND SETTING: Nineteen children from 6 to 12 years old at the time of the research having a brain-injured parent living at home and with cognitive impairments. MAIN OUTCOME MEASURES: Case report. Assessment of a questionnaire measures of anxiety, the R-CMAS scale. Qualitative analysis of a semi-structured interview and of the family drawing. RESULTS: Four children (21%) presented pathological anxiety assessed by the R-CMAS scale. The analysis of the semi-structured interview showed that 16 children had a representation of the brain injury. The symbolic place of the brain-injured parent was maintained for all the children and one presented impulsive behaviours. The family drawing analysis showed the lack of relational interaction between the family members in 16 cases (84%). Three children (15%) represented the real disability, and 17 (89%) abnormalities in the bodies' pictorial representation of the personages. These abnormalities concerned the brain-injured parent and the other members of the family. A characteristic sign was the lack of hands or the representation of amputee hands in 14 cases (73%). Another one was the unsteadiness of family members, who were also represented as ghosts or "in the air" in 13 cases (68%). CONCLUSION: Children seem adapted and they have few emotional and behavioural disorders. But there was a strong impact of the disability of the parent on their personal experience and on their perception of "the family body".


Subject(s)
Brain Injuries , Child of Impaired Parents , Surveys and Questionnaires , Child of Impaired Parents/psychology , Family Characteristics , Female , Humans , Infant , Male
3.
J Virol ; 75(19): 9177-86, 2001 Oct.
Article in English | MEDLINE | ID: mdl-11533181

ABSTRACT

Human immunodeficiency virus-type I (HIV-1) infection elicits antibodies (Abs) directed against several regions of the gp120 and gp41 envelope glycoproteins. Many of these Abs are able to neutralize T-cell-line-adapted strains (TCLA) of HIV-1, but only a few effectively neutralize primary HIV-1 isolates. The nature of HIV-1 neutralization has been carefully studied using human monoclonal Abs (MAbs), and the ability of such MAbs to act in synergy to neutralize HIV-1 has also been extensively studied. However, most synergy studies have been conducted using TCLA strains. To determine the nature of Ab interaction in HIV-1 primary isolate neutralization, a panel of 12 anti-HIV-1 human immunoglobulin G (IgG) MAbs, specific for epitopes in gp120 and gp41, were used. Initial tests showed that six of these MAbs, as well as sCD4, used individually, were able to neutralize the dualtropic primary isolate HIV-1(89.6); MAbs giving significant neutralization at 2 to 10 microg/ml included 2F5 (anti-gp41), 50-69 (anti-gp41), IgG1b12 (anti-gp120(CD4bd)), 447-52D (anti-gp120(V3)), 2G12 (anti-gp120), and 670-D (anti-gp120(C5)). For studies of reagent interaction, 16 binary combinations of reagents were tested for their ability to neutralize HIV-1(89.6). Reagent combinations tested included one neutralizing MAb with sCD4, six pairs consisting of two neutralizing MAbs, and nine pairs consisting of one neutralizing MAb with another non-neutralizing MAb. To assess the interaction of the latter type of combination, a new mathematical treatment of reagent interaction was developed since previously used methods could be used only when both reagents neutralize. Synergy was noted between sCD4 and a neutralizing anti-gp120(V3) MAb. Antagonism was noted between two pairs of anti-gp41 MAbs (one neutralizing and one non-neutralizing). All of the other 13 pairs of MAbs tested displayed only additive effects. These studies suggest that Abs rarely act in synergy to neutralize primary isolate HIV-1(89.6); many anti-HIV-1 Abs act additively to mediate this biological function.


Subject(s)
Antibody Specificity , HIV Antibodies/immunology , HIV Infections/virology , HIV-1/immunology , Cell Line , HIV Infections/immunology , Humans
4.
J Virol ; 74(21): 10025-33, 2000 Nov.
Article in English | MEDLINE | ID: mdl-11024131

ABSTRACT

A human immunodeficiency virus (HIV) vaccine that will be useful in diverse geographic regions will need to induce a broad immune response characterized by cross-clade immunity. To test whether a clade B-based HIV candidate vaccine could induce interclade humoral responses, including neutralizing activity against primary HIV-1 isolates, sera were tested from recipients of a vaccine consisting of recombinant canarypox virus vCP205 and recombinant gp120(SF2). Serum antibodies exhibited strong immunochemical cross-reactivity with V3 peptides from clades B, C, and F, with weaker activity for several V3 peptides from clades A, D, G, and H; essentially no reactivity could be demonstrated with V3 peptides from clades E and O. Extensive cross-clade reactivity was also documented by enzyme-linked immunosorbent assay with all nine recombinant HIV envelope glycoproteins tested from clades B, D, and E. In addition, vaccinees' sera displayed significant neutralizing activity against 5 of 14 primary isolates tested, including one X4 virus and two dualtropic viruses (from clade B) and two R5 viruses (from clades B and C). This is the first demonstration of the induction by a candidate HIV vaccine constructed from clade B laboratory strains of HIV of neutralizing activity against R5 and clade C primary isolates. The data suggest that, by virtue of their ability to induce cross-clade immune responses, appropriately formulated HIV vaccines based on a finite number of HIV isolates may ultimately be able to protect against the wide range of HIV isolates affecting the populations of many geographic regions.


Subject(s)
AIDS Vaccines/immunology , HIV Antibodies/immunology , HIV-1/immunology , Immunization, Secondary , Adolescent , Adult , Cross Reactions , Female , Gene Products, env/genetics , Gene Products, env/immunology , HIV Antibodies/blood , HIV Envelope Protein gp120/immunology , HIV Infections/prevention & control , HIV-1/classification , Humans , Male , Middle Aged , Neutralization Tests , Peptide Fragments/immunology , Recombinant Proteins/immunology , Vaccines, Synthetic/immunology
5.
Bull Acad Natl Med ; 184(1): 67-84; discussion 85-7, 2000.
Article in French | MEDLINE | ID: mdl-10989532

ABSTRACT

Six Rhesus macaques were hyperimmunized with either live infectious human immunodeficiency virus type 1 (HIV-1) or with beta-propiolactone--or formalin--inactivated HIV-1. The virus used was HIV-1 BX08, a primary virus isolate grown in human PBMC. Instead of eliciting virus-neutralizing antibodies, this regimen induced antibodies that enhanced HIV-1 infectivity for PBMC by 10 to 90 fold. Enhancement was also seen in a cell-to-cell fusion assay using a Semliki Forest virus replicon to express BX08 gp160 in CD4+, CCR5+ HeLa cell cultures. These observations raise the concern that whole virus particles-based HIV-1 vaccines might elicit enhancing antibodies that could play a facilitating role in the transmission and/or evolution of the disease.


Subject(s)
Antibody-Dependent Enhancement/immunology , HIV-1/immunology , Immunization , Macaca/immunology , Virion/isolation & purification , Animals , Male
6.
AIDS Res Hum Retroviruses ; 15(8): 731-43, 1999 May 20.
Article in English | MEDLINE | ID: mdl-10357469

ABSTRACT

Macrophage (M)-tropic HIV-1 isolates use the beta-chemokine receptor CCR5 as a coreceptor for entry, while T cell line-adapted (TCLA) strains use CXCR4 and dual-tropic strains can use either CCR5 or CXCR4. To investigate the viral determinants involved in choice of coreceptor, we used a fusion assay based on the infection of CD4+ HeLa cells that express one or both coreceptors with Semliki Forest virus (SFV) recombinants expressing the native HIV-1 gp160 of a primary M-tropic isolate (HIV-1BX08), a TCLA isolate (HIV-1LAI), or a dual-tropic strain (HIV-1MN). We examined whether the V3 region of these glycoproteins interacts directly with the corresponding coreceptors by assaying coreceptor-dependent cell-to-cell fusion mediated by the different recombinants in the presence of various synthetic linear peptides. Synthetic peptides corresponding to different V3 loop sequences blocked syncytium formation in a coreceptor-specific manner. Synthetic V2 peptides were also inhibitory for syncytium formation, but showed no apparent coreceptor specificity. A BX08 V3 peptide with a D320 --> R substitution retained no inhibitory capacity for BX08 Env-mediated cell-to-cell fusion, but inhibited LAI Env-mediated fusion as efficiently as the homologous LAI V3 peptide. The same mutation engineered in the BX08 env gene rendered it able to form syncytia on CD4+CXCR4+CCR5-HeLa cells and susceptible to inhibition by SDF-1alpha and MIP-1beta. Other substitutions tested (D320 --> Q/D324 --> N or S306 --> R) exhibited intermediate effects on coreceptor usage. These results underscore the importance of the V3 loop in modulating coreceptor choice and show that single amino acid modifications in V3 can dramatically modify coreceptor usage. Moreover, they provide evidence that linear V3 loop peptides can compete with intact cell surface-expressed gp120/gp41 for CCR5 or CXCR4 interaction.


Subject(s)
HIV Envelope Protein gp120/metabolism , HIV-1/physiology , Peptide Fragments/metabolism , Receptors, CCR5/metabolism , Receptors, CXCR4/metabolism , Amino Acid Sequence , Amino Acid Substitution , Giant Cells/physiology , HIV Envelope Protein gp120/chemistry , HIV Envelope Protein gp120/genetics , HIV-1/genetics , HeLa Cells , Humans , Molecular Sequence Data , Mutagenesis, Site-Directed , Peptide Fragments/chemistry , Peptide Fragments/genetics , Recombinant Proteins/metabolism , Structure-Activity Relationship
7.
Eur J Immunol ; 28(12): 4177-87, 1998 12.
Article in English | MEDLINE | ID: mdl-9862354

ABSTRACT

Chimeric T cell receptors (cTCR) with an antibody specificity have been proposed in several models as a combination of antibody and cellular immunotherapy without MHC restriction. Such a tool could be of a limited use in HIV infection because of the great variability of the virus. The human single-chain antibody (ScFv-b12) derives from the b12 antibody directed to the CD4 binding site of gp120, a potent neutralizer of different HIV-1 strains, including a large panel of primary isolates. A single-chain fragment variable (ScFv) bearing the VH Pro-->Glu mutation that improves b12 affinity 54-fold, called ScFv-b12E, was also constructed. The ScFv were linked to the signal-transducing y chain of the Fc(gamma)RIII, with or without spacer region, and expressed in the murine MD45 T cell line. The different cTCR formats behave similarly in terms of ScFv surface expression, but differ according to their activation threshold. T cell transfectants can be stimulated with immobilized gp120 derived from all HIV strains tested. BHK cells infected with Semliki forest virus (SFV) carrying an HIV-1 envelope gene (SFV-env) derived from either HIV-1 laboratory strains (LAI, MN12, HXB2) or field isolates (BX08, CHAR or 133) were used as targets for the transfectants. All gp120-expressing cells induced cTCR-specific activation. The latter result is contrasting with the lack of specific recognition of SFV-CHAR- or 133-infected cells by the native b12 antibody, as measured by cytofluorometric analysis. Finally, HeLa cells (which constitutively express the coreceptor CXCR4) are able to bind HIV-1 gp160 when transfected with the chimeric receptor ScFv-b12-gamma, but, importantly, do not become infected by the virus. Our results therefore suggest that cTCR with b12 specificity can confer to T cells broad anti-HIV reactivity without making them susceptible to HIV infection.


Subject(s)
CD4 Antigens/immunology , HIV Envelope Protein gp120/immunology , Receptors, Antigen, T-Cell/immunology , Recombinant Fusion Proteins/immunology , T-Lymphocytes/immunology , Antibody Specificity , Binding Sites/immunology , HIV Envelope Protein gp120/genetics , HeLa Cells , Humans , Immunoglobulins/immunology , Receptors, Antigen, T-Cell/genetics , Recombinant Fusion Proteins/genetics , Transfection
8.
Proc Natl Acad Sci U S A ; 94(17): 9326-31, 1997 Aug 19.
Article in English | MEDLINE | ID: mdl-9256481

ABSTRACT

The beta-chemokine receptor CCR-5 is essential for the efficient entry of primary macrophage-tropic HIV-1 isolates into CD4(+) target cells. To study CCR-5-dependent cell-to-cell fusion, we have developed an assay system based on the infection of CD4(+) CCR-5(+) HeLa cells with a Semliki Forest virus recombinant expressing the gp120/gp41 envelope (Env) from a primary clade B HIV-1 isolate (BX08), or from a laboratory T cell line-adapted strain (LAI). In this system, gp120/gp41 of the "nonsyncytium-inducing," primary, macrophage-tropic HIV-1BX08 isolate, was at least as fusogenic as that of the "syncytium-inducing" HIV-1LAI strain. BX08 Env-mediated fusion was inhibited by the beta-chemokines RANTES (regulated upon activation, normal T cell expressed and secreted) and macrophage inflammatory proteins 1beta (MIP-1beta) and by antibodies to CD4, whereas LAI Env-mediated fusion was insensitive to these beta-chemokines. In contrast soluble CD4 significantly reduced LAI, but not BX08 Env-mediated fusion, suggesting that the primary isolate Env glycoprotein has a reduced affinity for CD4. The domains in gp120/gp41 involved in the interaction with the CD4 and CCR-5 molecules were probed using monoclonal antibodies. For the antibodies tested here, the greatest inhibition of fusion was observed with those directed to conformation-dependent, rather than linear epitopes. Efficient inhibition of fusion was not restricted to epitopes in any one domain of gp120/gp41. The assay was sufficiently sensitive to distinguish between antibody- and beta-chemokine-mediated fusion inhibition using serum samples from patient BX08, suggesting that the system may be useful for screening human sera for the presence of biologically significant antibodies.


Subject(s)
Antibodies, Viral/immunology , Epitopes/immunology , HIV Envelope Protein gp120/immunology , HIV-1 , Macrophages/virology , Receptors, Cytokine/immunology , Receptors, HIV/immunology , Antibodies, Viral/pharmacology , Antibody Specificity , Cell Fusion/drug effects , Cell Fusion/immunology , HIV Envelope Protein gp120/chemistry , HeLa Cells , Humans , Macrophages/immunology , Macrophages/pathology , Protein Conformation , Receptors, CCR5
9.
Virology ; 232(1): 98-104, 1997 May 26.
Article in English | MEDLINE | ID: mdl-9185593

ABSTRACT

To evaluate the potential protective efficacy of a live recombinant human immunodeficiency virus type 1 (HIV-1) canarypox vaccine candidate, two chimpanzees were immunized five times with ALVAC-HIV-1 vCP250, a recombinant canarypox virus that expresses the HIV-1[IIIB(LAI)] gp120/TM, gag, and protease gene products. One month after the last booster inoculation, the animals were challenged by intravenous injection of cell-associated virus in the form of peripheral blood mononuclear cells from an HIV-1[IIIB(LAI)]-infected chimpanzee. One chimpanzee with a neutralizing antibody titer to HIV-1[IIIB(LAI)] of 128 at the time of challenge was protected, whereas both the second animal, with a neutralizing antibody titer of 32, and a naive control animal became infected. At 5 months after challenge, the protected chimpanzee and a third animal, previously immunized with various HIV-1[MN] antigens, were given a booster inoculation. The two animals were challenged intravenously 5 weeks later with twenty 50% tissue culture infectious doses of cell-free HIV-1[DH12], a heterologous subtype B isolate. Neither chimpanzee had neutralizing antibodies to HIV-1[DH12], and neither one was protected from infection with this isolate. The immune responses elicited by vaccination against HIV-1[IIIB(LAI)] or HIV-1[MN] did not, therefore, protect the animals from challenge with the heterologous cell-free HIV-1[DH12].


Subject(s)
AIDS Vaccines/immunology , HIV Infections/prevention & control , Vaccines, Synthetic/immunology , Viral Vaccines/immunology , AIDS Vaccines/administration & dosage , Animals , Avipoxvirus/genetics , HIV Antibodies/biosynthesis , HIV Infections/immunology , HIV-1/immunology , Immunoenzyme Techniques , Male , Neutralization Tests , Pan troglodytes , Vaccines, Synthetic/administration & dosage , Viral Vaccines/administration & dosage
10.
Curr Microbiol ; 32(1): 38-42, 1996 Jan.
Article in English | MEDLINE | ID: mdl-8555942

ABSTRACT

The plasma membrane of Mycoplasma mycoides subsp. mycoides SC (strain KH3J) contains over 160 polypeptides with apparent molecular masses ranging from 14 to 125 kDa and isoelectric point values (pIs) from 5 to 9. In vivo labeling with [14C]-fatty acids revealed about 35 acylated polypeptides including the two major components p42 and p65 and displaying pIs between 5.5 and 9.0, with a majority between 6.5 and 8. The amphiphilic nature of most of these acyl proteins was confirmed by Triton X-114 phase partitioning. Gas-liquid chromatography analyses showed that the order of preference for protein acylation was 16:0 > 18:2c > 18:1c > 18:0 > 14:0, with 16:0 being the major O-ester-bound fatty acyl chain and 18:2c the major N-linked chain. The presence of S-glycerylcysteine and a ratio of [O-ester-bound acyl chains + N-linked chains]/O-ester bound chains of approximately 1.2 in M. mycoides subsp. mycoides SC membrane proteins are consistent with a lipid modification similar to that occurring in lipoproteins of Gram-negative eubacteria that contain an N-terminal acyl S-glycerylcysteine.


Subject(s)
Membrane Proteins/metabolism , Mycoplasma mycoides/metabolism , Pleuropneumonia/microbiology , Acylation , Animals , Cattle
11.
Pathol Biol (Paris) ; 40(1): 47-51, 1992 Jan.
Article in French | MEDLINE | ID: mdl-1570182

ABSTRACT

An eosinophilic granuloma was found in the operative specimen from a patient who underwent colonic resection eleven days after onset of abdominal pain. Upon questioning, the patient reported having eaten raw fish eggs (cod) on the day before the onset of abdominal pain. Colonic localization of this anisakiasis, although more common in Europe than in Japan, is nevertheless infrequent, with only 17 other cases having been published to date. Eosinophil counts rose after 15 days and specific serologic tests became positive after 21 days with titers remaining detectable longer by Western blot (31 months) than by immunoelectrophoresis (2 months). Routine serologic tests for anisakiasis in patients with eosinophilic granulomas of the digestive tract would ensure the correct etiological diagnosis in some cases.


Subject(s)
Colonic Diseases/parasitology , Eggs , Eosinophilic Granuloma/parasitology , Nematoda/isolation & purification , Nematode Infections/parasitology , Adult , Animals , Antigens, Helminth/analysis , Colonic Diseases/blood , Colonic Diseases/surgery , Eosinophilic Granuloma/blood , Eosinophilic Granuloma/surgery , Eosinophils , Fishes/parasitology , Food Parasitology , Humans , Immunoglobulin E/analysis , Male , Nematode Infections/blood , Nematode Infections/immunology , Nematode Infections/surgery
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