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1.
Public Health ; 213: 61-67, 2022 Dec.
Article in English | MEDLINE | ID: mdl-36371953

ABSTRACT

OBJECTIVE: We aimed to describe studies on human papillomavirus (HPV) vaccination education strategies from low- and middle-income countries in the published literature that could be applicable in Sub-Sahara Africa. STUDY DESIGN: This scoping review was guided by Arksey and O'Malley's methodological framework advanced by Levac et al. METHODS: We searched four electronic health sciences databases for relevant reports published between January 2006 and January 2021. Two reviewers screened for inclusion and extracted data for analysis and synthesis. Descriptive statistics and narrative descriptions were used to summarize the findings. RESULTS: The database search retrieved 1757 reports, of which 48 were from low- and middle-income countries and met the inclusion criteria. Of these, there were 39 interventional studies (81.3%). Less than one-fifth of the studies (n = 9) reported a theoretical basis for their strategies. Most strategies sought to improve knowledge and awareness about HPV (75%, n = 36), whereas outcomes for the remaining studies were related to increasing HPV vaccine acceptability. HPV education strategies (1) primarily targeted females, (2) were mostly provided by health professionals, and (3) used various modalities of learning, including in-person sessions, text-based materials, media, theater, and online delivery. CONCLUSIONS: HPV educational strategies are underresearched in most LMICs, suggesting the need for more primary observational, interventional, and experimental research, as well as program evaluations, focused on HPV educational strategies and theoretically informed. Once additional studies are added to the body of evidence, it will be valuable to review and synthesize diverse sources of evidence to determine what educational strategies are most useful and have the greatest impact on HPV vaccination in these settings, particularly Sub-Saharan Africa.


Subject(s)
Papillomavirus Infections , Papillomavirus Vaccines , Humans , Human Papillomavirus Viruses , Papillomavirus Infections/prevention & control , Developing Countries
2.
J Mol Recognit ; 13(6): 382-7, 2000.
Article in English | MEDLINE | ID: mdl-11114071

ABSTRACT

This study investigated the potential to utilize phage-displayed peptides as reagents in sensor applications. A library of random 12-mers displayed on phage was panned against staphylococcal enterotoxin B (SEB), a causative agent of food poisoning. Nine SEB binding phage clones were isolated, all of which share the consensus sequence Trp His Lys at their amino terminus. Binding of several of these phage was shown to be inhibited when they were assayed in a competitive enzyme-linked immunosorbent assay (ELISA) format with synthesized peptide corresponding to the peptide-encoding region of one of the clones. Whole phage were labeled with the dye Cy5, and incorporated into fluoroimmunoassays. Labeled phage were able to detect SEB down to a concentration of 1.4 ng/well in a fluorescence-based immunoassay. When incorporated into an automated fluorescence-based sensing assay, Cy5-labeled phage bound to probes coated with SEB generated a robust signal of about 10,000 pA, vs a signal of 1,000 pA using a control fiber coated with streptavidin. These results demonstrate the potential for development of phage-based sensor reagents.


Subject(s)
Biosensing Techniques , Enterotoxins/metabolism , Peptide Library , Peptides/metabolism , Bacteriophage M13 , Enzyme-Linked Immunosorbent Assay , Fiber Optic Technology , Fluoroimmunoassay/methods , Indicators and Reagents , Peptides/chemical synthesis , Peptides/isolation & purification , Protein Binding , Staphylococcus aureus
3.
Biosens Bioelectron ; 14(10-11): 771-7, 2000 Jan.
Article in English | MEDLINE | ID: mdl-10945451

ABSTRACT

The capabilities of the portable, automated fiber optic biosensor, RAPTOR, have recently been evaluated. Developed to perform rapid fluoroimmunoassays in the field, the RAPTOR was designed to test samples for up to four different target analytes simultaneously. Assay time could be varied from a 3-min rapid screen to a standard 10-min test. A trial of 203 blind samples tested for Staphylococcal enterotoxin B, ricin, Francisella tularensis, and Bacillus globigii has been conducted. Sensitivities obtained were 10, 50 ng/ml, 5 x 10(5), and 5 x 10(4) cfu/ml, respectively.


Subject(s)
Biosensing Techniques , Immunoassay , Bacillus/isolation & purification , Enterotoxins/analysis , Fiber Optic Technology , Francisella tularensis/isolation & purification , Optical Fibers , Ricin/analysis , Sensitivity and Specificity
4.
Biosens Bioelectron ; 14(2): 163-70, 1999 Feb.
Article in English | MEDLINE | ID: mdl-10101838

ABSTRACT

The Man-portable Analyte Identification System (MANTIS), the first fully automated, self-contained, portable fiber optic biosensor, was utilized for the detection of Staphylococcal Enterotoxin B (SEB), a bacterial toxin produced by Staphylococcus aureus that commonly causes food poisoning. Because of its remarkable toxicity and stability, SEB is considered a prime threat as a biological weapon of mass destruction. The assay for SEB was used to evaluate the MANTIS' ability to function in the presence of various environmental interferents. The sensor could reliably detect SEB spiked into liquid samples containing a variety of smoke particles. However, substantial interference occurred when SEB was mixed into matrices capable of adsorbing SEB, such as 1% solutions of clay, topsoil, or pollen. Of equal importance, none of the interferents produced false positives in the MANTIS. The MANTIS demonstrated the capability to perform simultaneous immunoassays rapidly in the field with little or no user intervention.


Subject(s)
Biosensing Techniques , Enterotoxins/analysis , Staphylococcus aureus/pathogenicity , Fiber Optic Technology , Fluoroimmunoassay , Optical Fibers
5.
Clin Diagn Lab Immunol ; 5(5): 609-12, 1998 Sep.
Article in English | MEDLINE | ID: mdl-9729524

ABSTRACT

The fiber-optic biosensor, originally developed to detect hazardous biological agents such as protein toxins or bacterial cells, has been utilized to quantify the concentration of serum antiplague antibodies. This biosensor has been used to detect and quantify the plague fraction 1 antigen in serum, plasma, and whole-blood samples, but its ability to quantify serum antibodies has not been demonstrated. By using a competitive assay, the concentration of serum antiplague antibodies was ascertained in the range of 2 to 15 microgram/ml. By making simple dilutions, concentrations for 11 serum samples whose antiplague antibody concentrations were unknown were determined and were found to be in good agreement with enzyme-linked immunosorbent assay results. The competitive assay method could be used to effectively determine the exposure to plague of animals or humans or could be applied to other diseases, such as hepatitis or AIDS, where the presence of antibodies is used to diagnose infection.


Subject(s)
Antibodies, Bacterial/blood , Biosensing Techniques , Fiber Optic Technology/instrumentation , Plague/diagnosis , Yersinia pestis/immunology , Animals , Bacterial Proteins/immunology , Fluoroimmunoassay/methods , Humans , Immunoenzyme Techniques , Optical Fibers , Plague/immunology , Plague/microbiology , Rabbits , Yersinia pestis/isolation & purification
6.
Cell Immunol ; 185(2): 123-33, 1998 May 01.
Article in English | MEDLINE | ID: mdl-9636690

ABSTRACT

A thymic epithelial cell line (tsTNC-1) that maintains the ability to selectively bind and internalize immature alpha beta TCRloCD4+CD8+ thymocytes in vitro was used in the development of a monoclonal antibody that is specific to the cell surface of thymic nurse cells (TNCs) in the thymus. The rat monoclonal antibody ph91 showed specificity to cells of the subcapsular region of the thymic cortex. Upon mechanical dispersion of the thymus in vitro, ph91 recognized cells displaying the multicellular morphology unique to TNCs. Ph91 staining was not detected on fresh thymocytes, stromal cells of the inner thymic cortex, thymic medullary cells, B cells or fibroblasts. Ph91 recognized a 43-kDa protein on the surface of TNCs. Exposure of tsTNC-1 cells to ph91 in tissue culture significantly reduced the percentage of binding of the alpha beta TCRloCD4+CD8+ thymocyte subset previously shown to target TNCs. In organ culture, ph91 reduced the viability of developing thymocytes by 70%. The largest reduction was found in the alpha beta TCR+CD4+CD8+ thymocyte subset. These results represent the first report of a TNC-specific monoclonal antibody. Further, the antigen to which ph91 binds may play a role in the process of thymocyte binding and their subsequent internalization which is unique to TNCs and important to the T cell developmental process.


Subject(s)
Antibodies, Monoclonal/chemistry , Antibody Specificity , Thymus Gland/cytology , Thymus Gland/immunology , Animals , Antibodies, Monoclonal/isolation & purification , Antibodies, Monoclonal/pharmacology , Cell Adhesion/immunology , Cell Differentiation/immunology , Cell Line, Transformed , Epithelial Cells , Epitopes/immunology , Fluorescent Antibody Technique, Indirect , Growth Inhibitors/pharmacology , Mice , Mice, Inbred C57BL , Molecular Weight , Organ Culture Techniques , Organ Specificity/immunology , Staining and Labeling , T-Lymphocytes/immunology , Thymus Gland/metabolism
7.
Biosens Bioelectron ; 12(4): 329-36, 1997.
Article in English | MEDLINE | ID: mdl-9178518

ABSTRACT

The fiber optic biosensor performs fluoroimmunoassays at the surface of multimode optical fibers. The effectiveness of protein A, an immunoglobulin binding protein, for antibody immobilization on the surface of these fiber probes has been investigated. No difference was observed in the binding of fluorescently-labeled goat-IgG by rabbit anti-goat IgG regardless of whether the capture antibody was bound to the probe surface via protein A or covalently attached. However, in a sandwich immunoassay for the F1 antigen of Yersinia pestis, probes with rabbit anti-plague IgG bound to the surface via protein A generated twice the signal as probes with the antibody covalently attached. Assay regeneration was also examined with protein A probes since antibody-antigen complexes have been successfully eluted from protein A under low pH conditions. Protein A probes coated with rabbit anti-goat IgG obtained nearly identical signal levels at 500 and 5000 ng/ml of Cy5.5 goat IgG five consecutive times following regeneration with glycine-HCl, 2% acetic acid, pH 2.5.


Subject(s)
Antigen-Antibody Reactions , Biosensing Techniques , Fiber Optic Technology , Fluoroimmunoassay/methods , Staphylococcal Protein A/immunology , Immunoglobulin G/immunology , Optical Fibers
8.
Anal Biochem ; 233(1): 50-7, 1996 Jan 01.
Article in English | MEDLINE | ID: mdl-8789146

ABSTRACT

A new, portable fiber-optic biosensor has been used to detect staphylococcal enterotoxin B, a causative agent of food poisoning, at levels as low as 0.5 ng/ml in buffer. The toxin (SEB) can also be detected and quantitated in other relevant media: human serum, urine, and aqueous extract of ham. The level of toxin, from 5 to 200 ng/ml, can be accurately predicted in these media by calibrating each fiber and by comparing results to a single standard curve based on toxin in buffer. The quantitative fluorescent sandwich immunoassay provides results in 45 min; qualitative results are provided in 15-20 min. Using a blender and a benchtop centrifuge, fast, simple aqueous extracts of contaminated ham samples were prepared and tested. Ham spiked with 5 or 40 micrograms SEB per 100 g food resulted in biosensor readings indicative of 11 or 69% recovery of the toxin, respectively. Finally, the SEB assay is highly specific; SEA and SED give only 2-3% of the signal at 5000 ng/ml as SEB gives at 1000 ng/ml. This specific, sensitive assay for SEB on the portable fiber-optic biosensor permits easy monitoring of clinical samples or on-site analysis of suspect food samples.


Subject(s)
Biosensing Techniques , Enterotoxins/analysis , Fiber Optic Technology , Fluoroimmunoassay/methods , Animals , Buffers , Enterotoxins/blood , Enterotoxins/urine , Evaluation Studies as Topic , Food Microbiology , Humans , Meat/analysis , Meat/microbiology , Optical Fibers , Staphylococcal Food Poisoning/blood , Staphylococcal Food Poisoning/diagnosis , Staphylococcal Food Poisoning/urine , Staphylococcus aureus , Swine
9.
J Neurochem ; 56(1): 163-71, 1991 Jan.
Article in English | MEDLINE | ID: mdl-1702830

ABSTRACT

The mouse myelin proteolipid protein (PLP) gene has been studied in normal and jimpymsd mice. Potential upstream regulatory regions of the normal gene have been cloned and mapped, but when these regions were studied in jimpymsd mice by Southern blots, no alterations were observed, relative to the normal gene. To assess whether the low ratio of PLP to DM20 proteins in this mutant reflected an altered PLP/DM20 ratio mRNAs, S1 nuclease analyses were undertaken, which demonstrated that at all ages studied in both jimpy and jimpymsd mice, PLP mRNA was elevated above DM20 mRNA. When exon 3 (the site of the alternative splice signal for DM20 mRNA) of the jimpymsd PLP gene was sequenced, no mutation was identified. The transcription of the PLP gene in normal and mutant animals was studied. The transcription rate increases in normal animals with development, and in very young jimpymsd or jimpy mice, the transcription rate of the PLP gene was close to that of age-matched normal animals. However, by 10 days of age, the transcription rate of this gene in both mutants was significantly below that of age-matched controls. The transcription rate of the myelin basic protein (MBP) gene was also reduced, indicating that expression of both genes is affected by this mutation. In contrast, the transcription rate of the glycerol phosphate dehydrogenase (GPDH) gene, an early marker of oligodendrocytes, is equal to or greater than normal in both mutants. We have confirmed an earlier report of a point mutation in exon 6 of the jimpymsd PLP gene, which converts an alanine to a valine.(ABSTRACT TRUNCATED AT 250 WORDS)


Subject(s)
Gene Expression , Mutation , Myelin Proteins/genetics , Nerve Tissue Proteins , Oligodendroglia/metabolism , Amino Acid Sequence , Animals , Base Sequence , Cloning, Molecular , Exons , Mice , Mice, Mutant Strains , Molecular Sequence Data , Myelin Proteolipid Protein , Proteolipids/genetics , RNA Splicing , RNA, Messenger/metabolism , Regulatory Sequences, Nucleic Acid , Restriction Mapping , Single-Strand Specific DNA and RNA Endonucleases/metabolism , Transcription, Genetic
10.
FEBS Lett ; 223(2): 417-21, 1987 Nov 02.
Article in English | MEDLINE | ID: mdl-2444462

ABSTRACT

The myelin proteolipid protein gene was characterized in jimpy mice to identify the specific mutation that produces dysmyelination, oligodendrocyte cell death, and death of the animal by 30 days of age. Exon 5 and flanking intron segments were isolated from jimpy proteolipid protein genomic clones and sequenced. A single nucleotide difference was noted between the normal and jimpy proteolipid protein genes: the conversion of an AG/GT to a GG/GT in the splice acceptor signal preceding exon 5, which apparently destroys the splice signal. Thus, exon 5 of the mouse myelin proteolipid protein gene is skipped during the processing of mRNA, producing a shortened proteolipid protein mRNA.


Subject(s)
Mice, Jimpy/genetics , Mice, Neurologic Mutants/genetics , Myelin Proteins/genetics , RNA Splicing , Animals , Base Sequence , Exons , Genes , Mice , Molecular Sequence Data , Mutation , Myelin Proteolipid Protein , RNA, Messenger/genetics
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