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1.
Bull World Health Organ ; 90(9): 652-658B, 2012 Sep 01.
Article in English | MEDLINE | ID: mdl-22984309

ABSTRACT

OBJECTIVE: To describe recent changes in policy on provider-initiated testing and counselling (PITC) for human immunodeficiency virus (HIV) infection in African countries and to investigate patients' experiences of and views about PITC. METHODS: A review of the published literature and of national HIV testing policies, strategic frameworks, plans and other relevant documents was carried out. FINDINGS: Of the African countries reviewed, 42 (79.2%) had adopted a PITC policy. Of the 42, all recommended PITC for the prevention of mother-to-child HIV transmission, 66.7% recommended it for tuberculosis clinics and patients, and 45.2% for sexually transmitted infection clinics. Moreover, 43.6% adopted PITC in 2005 or 2006. The literature search identified 11 studies on patients' experiences of and views about PITC in clinical settings in Africa. The clear majority regarded PITC as acceptable. However, women in antenatal clinics were not always aware that they had the right to decline an HIV test. CONCLUSION: Policy and practice on HIV testing and counselling in Africa has shifted from a cautious approach that emphasizes confidentiality to greater acceptance of the routine offer of HIV testing. The introduction of PITC in clinical settings has contributed to increased HIV testing in several of these settings. Most patients regard PITC as acceptable. However, other approaches are needed to reach people who do not consult health-care services.


Subject(s)
AIDS Serodiagnosis/trends , Directive Counseling/methods , HIV Infections/diagnosis , Health Education/methods , Africa/epidemiology , Female , HIV Infections/epidemiology , HIV Infections/psychology , Health Promotion/methods , Humans , Infectious Disease Transmission, Vertical/prevention & control , Pregnancy , Public Health/methods
3.
Biosens Bioelectron ; 16(9-12): 945-53, 2001 Dec.
Article in English | MEDLINE | ID: mdl-11679274

ABSTRACT

This study was undertaken to synthesize peptides that are partially similar to the binding sites of human olfactory receptor protein. First, a putative 3-D model structure of human olfactory receptor protein (P30953) was modeled using a molecular simulation method. The computer docking simulation was then performed to determine the most plausible binding sites between the model structure and target gases, trimethylamine, ammonia, acetic acid, and o-xylene. According to the simulation result, a series of polypeptide sequences, horp61 for TMA, horp103 for o-xylene, horp109 for ammonia, and horp193 for acetic acid as recognized molecules were designed for gas sensing purposes. Preparing these peptides as corresponding gas sensing probes, the results showed a high relative sensitivity response of 6.7 for TMA (probe horp61), 5.1 for o-xylene (probe horp103), 11 for ammonia (probe horp109), and 28 for acetic acid (probe horp193), respectively. These results indicate that peptide mimicking of binding domain on olfactory receptor opens a new window and offers a novel strategy for the further development of recognized materials for gas sensing.


Subject(s)
Biosensing Techniques/methods , Gases/analysis , Molecular Mimicry , Amino Acid Sequence , Binding Sites , Humans , Models, Molecular , Molecular Sequence Data , Peptides/chemistry , Peptides/metabolism , Receptors, Odorant/chemistry , Receptors, Odorant/metabolism
4.
J Biotechnol ; 80(1): 63-73, 2000 Jun 09.
Article in English | MEDLINE | ID: mdl-10862987

ABSTRACT

A putative tertiary structure model of the dog's olfactory receptor (olfd canfa) is established in this study. By using a target odorous compound (trimethylamine), it is possible to locate the most plausible binding sites between the receptor model structure and the target odorous molecules through computer docking simulations. The two short oligo-peptide sequences (orp61 and orp188) for trimethylamine sensing were identified, synthesized, purified and coated onto the surface of the separate piezoelectric gold electrodes. These two peptides show a high binding capability for trimethylamine. To further enhance the sensitivity of the polypeptides towards the target compound, the polarity and the degree of docking were changed by a site-specific modification technique. The orp61 sequence was modified by substituting two amino acids in the binding pocket resulting in 33% increase in sensitivity towards trimethylamine and reduced noises from other non-target chemicals. The techniques used in the present study offer a unique approach for synthesizing peptides in mimicking binding domain of olfactory receptors. The approach can be easily applied to further development of recognized molecules for gas sensing, especially for use in 'electronic noses'.


Subject(s)
Models, Molecular , Molecular Mimicry , Peptides/chemical synthesis , Peptides/metabolism , Receptors, Odorant/chemical synthesis , Receptors, Odorant/metabolism , Amino Acid Sequence , Amino Acid Substitution , Animals , Binding Sites , Computer Simulation , Dogs , Gases/metabolism , Ligands , Methylamines/metabolism , Molecular Sequence Data , Peptides/chemistry , Protein Binding , Protein Structure, Secondary , Protein Structure, Tertiary , Receptors, Odorant/chemistry
5.
Biochem Mol Biol Int ; 44(3): 529-34, 1998 Mar.
Article in English | MEDLINE | ID: mdl-9556214

ABSTRACT

Two antibody preparations against cardiotoxins were raised by immunizing rabbits with cardiotoxin 1 and cardiotoxin 3, respectively. The two antibody preparations showed precipitin reactions with cardiotoxins 1, 2, 3 and 5, respectively. However, the results of competitive enzyme-linked immunoassay revealed that the respective cardiotoxin molecules exhibited different reactivity toward anticardiotoxin antibodies. Moreover, the order of reactivity with antibodies was not in line with the degree of their sequence identity. This suggest that the anticardiotoxin antibodies may recognize conformational epitopes rather than sequential ones in the toxin molecules. Alternatively, the four cardiotoxins reacted well with the antibodies in the absence of competitor, suggesting that sequence variations with cardiotoxin molecules may not exclusively influence the potential use of the anticardiotoxin antibodies for the neutralization of the activity of cardiotoxin variants.


Subject(s)
Antibodies/metabolism , Elapid Venoms/chemistry , Elapid Venoms/immunology , Amino Acid Sequence , Animals , Antibodies/immunology , Binding, Competitive , Cobra Cardiotoxin Proteins/chemistry , Cobra Cardiotoxin Proteins/immunology , Enzyme-Linked Immunosorbent Assay , Molecular Sequence Data , Protein Conformation , Rabbits , Sequence Homology, Amino Acid , Structure-Activity Relationship
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