Qualitative assessment of hand hygiene knowledge, attitudes and practices among healthcare workers prior to the implementation of the WHO Hand Hygiene Improvement Strategy at Faranah Regional Hospital, Guinea.

Healthcare-associated infections are a serious burden globally. Few qualitative studies have explored healthcare workers' knowledge, attitudes and practices of hand hygiene. Prior to the implementation of the World Health Organization's Hand Hygiene Improvement Strategy at Faranah Regional Hospital in the Upper Region of Guinea in December 2018, we conducted a qualitative baseline assessment of knowledge, attitudes and practices of hand hygiene among healthcare workers to guide future hand hygiene interventions.

Detection of Lassa virus in wild rodent feces: Implications for Lassa fever burden within households in the endemic region of Faranah, Guinea.

Lassa arenavirus (LASV) is the cause of Lassa Fever in humans in West Africa. The multimammate mouse () is a reservoir host of LASV and the primary source of human infections. Humans are assumed to become infected due to contact with this animal or its excretions.

Hunting and consumption of rodents by children in the Lassa fever endemic area of Faranah, Guinea.

As a consequence of the Ebola outbreak, human-animal contact has gained importance for zoonotic transmission surveillance. In Faranah (Upper Guinea), daily life is intertwined with rodents, such as the Natal multimammate mouse, Mastomys natalensis; a reservoir for Lassa virus (LASV). However, this contact is rarely perceived as a health risk by residents, although Lassa fever (LF) is known to be endemic to this region.

Complete protection of mice from respiratory syncytial virus infection following mucosal delivery of synthetic peptide vaccines.

We have previously shown that intraperitoneal immunization of BALB/c mice with the 14 amino-acid long synthetic peptides G/174-187 and BG/174-187, representing the region 174-187 of the G-glycoprotein from human (H) and bovine (B) respiratory syncytial virus (RSV), respectively, completely protects animals from infection with the corresponding virus. A current goal in vaccine development being the delivery of noninvasive protective antigens via mucosal surfaces, we have evaluated the immunogenicity and protective efficacy of the two peptides when administered to mice by the intranasal (i.n.

Clonal deletion of some V beta+ T cells in peripheral lymphocytes from C57BL/6 mice infected with MHV3.

Mouse hepatitis virus type 3 infection is generally accompanied by a severe immune dysfunction involving thymic or splenic T cell subpopulations. We postulate that the peripheral lymphoid cell depletions were caused by a selective deletion of some V beta subsets of mature T cells, as observed with superantigens. We have examined the expression of V beta 6, V beta 8 and V beta 14 in T cell subpopulations from the spleen and lymph nodes of pathogenic L2-MHV3-infected C57BL/6 mice.

Genomic and antigenic variations of porcine reproductive and respiratory syndrome virus major envelope GP5 glycoprotein.

The objective of the present study was to evaluate the importance of genomic and antigenic variations which may have affected the major envelope glycoprotein GP5 of porcine reproductive and respiratory syndrome virus (PRRSV) isolates responsible for outbreaks in Quebec and Ontario, in comparison with the modified-live U.S. vaccine strain (MLV) and the European prototype strain from Lelystad (LV).

A subset of porcine reproductive and respiratory syndrome virus GP3 glycoprotein is released into the culture medium of cells as a non-virion-associated and membrane-free (soluble) form.

The GP3 protein of the IAF-Klop strain of porcine reproductive and respiratory syndrome virus (PRRSV) was expressed in 293 cells by a recombinant human type 5 adenovirus carrying the open reading frame 3 gene. The protein exhibited a molecular mass of 42 kDa and comigrated with GP3 expressed in PRRSV-infected MARC-145 cells. Removal of N-linked glycans from GP3 resulted in a 27-kDa protein (P3), confirming its highly glycosylated nature.

Immune response in pigs vaccinated with plasmid DNA encoding ORF5 of porcine reproductive and respiratory syndrome virus.

The ORF5-encoded major envelope glycoprotein (GP5) of porcine reproductive and respiratory syndrome virus (PRRSV) is one of the three major structural proteins of this virus. While some porcine convalescent sera and monoclonal antibodies directed against GP4 and GP5 have the capacity to neutralize the virus in vitro, the protein specificity of porcine neutralizing sera has not yet been established. DNA immunization with a plasmid encoding GP5 of PRRSV, under the control of a human cytomegalovirus promoter, induced anti-GP5-specific neutralizing antibodies in pigs and BALB/c mice.

Differentiation between porcine reproductive and respiratory syndrome virus isolates by restriction fragment length polymorphism of their ORFs 6 and 7 genes.

Three distinct antigenic profiles were identified by comparing the reactivities of 15 Canadian field isolates, the attenuated U.S. vaccine (Ingelvac MLV) strain and 2 European reference strains (Lelystad and Weybridge) of the porcine reproductive and respiratory syndrome virus (PRRSV) by indirect immunofluorescence with a set of 4 monoclonal antibodies to the nucleocapsid (N) protein and 2 other to the matrix (M) protein.

Sequence analysis and expression of the polyhedrin gene of Choristoneura fumiferana cytoplasmic polyhedrosis virus (CfCPV).

The segmented double-stranded RNA genome of Choristoneura fumiferana cytoplasmic polyhedrosis virus (CfCPV) was extracted, polyadenylated, reverse-transcribed into cDNA and cloned. The cDNA clones that hybridized to the smallest genomic segment (segment 10) were identified, and its nucleotide sequence was determined. Genome segment 10 of CfCPV was found to be 1171 nucleotides in length with a single open reading frame in one strand capable of coding a predicted protein of 258 residues (Mr of 29,795), consistent with an apparent Mr of 30.

Immunization with a peptide derived from the G glycoprotein of bovine respiratory syncytial virus (BRSV) reduces the incidence of BRSV-associated pneumonia in the natural host.

Previous reports demonstrate that synthetic peptides corresponding to the amino acid region 174-187 of G glycoprotein from subgroups A and B human respiratory syncytial virus (HRSV), containing a Cys-->Ser substitution at position 186, confer complete resistance to immunized BALB/c mice against infection with the respective virus. In this report, we show that a Cys186-->Ser substituted peptide (BG/174-187) representing the corresponding region of the bovine (B) RSV G glycoprotein conferred complete protection of mice against BRSV challenge, suggesting that the 174-187 region of RSV G glycoproteins constitutes a dominant protective epitope which has been maintained throughout evolution. Furthermore, immunization of calves with peptide BG/174-187 efficiently induced the production of antibodies capable of recognizing both the parental G glycoprotein and peptide BG/174-187.

Monoclonal antibodies to the ORF5 product of porcine reproductive and respiratory syndrome virus define linear neutralizing determinants.

Complementary DNA encoding the ORF5 gene of a Quebec reference isolate (IAF-Klop) of porcine reproductive and respiratory syndrome virus (PRRSV) was cloned into the prokaryotic expression vectors pGEX-4T and pET21a to produce ORF5-glutathione S-transferase and ORF5-polyhistidine fusion proteins. Five hybridoma cell lines producing monoclonal antibodies (MAbs) to the 25 kDa viral envelope glycoprotein (GP5) were obtained from BALB/c mice immunized with the affinity chromatography-purified GST-ORF5 fusion protein. The polypeptide specificity of these anti-PRRSV MAbs, belonging to the IgG1 isotype, was confirmed by Western immunoblotting assays with recombinant and native viral proteins, and by radioimmunoprecipitation using [35S]methionine-labelled concentrated extracellular virus.

Protective immune responses induced by the immunization of mice with a recombinant bacteriophage displaying an epitope of the human respiratory syncytial virus.

We investigated whether a recombinant bacteriophage displaying a disease-specific protective epitope could be experimentally used as a vaccine to confer protection of immunized animals against infection. We genetically engineered a recombinant phage, fd, displaying at its surface a chimeric pIII coat protein fused to the previously identified protective epitope 173-187 from the glycoprotein G of the human respiratory syncytial virus (RSV). A selected recombinant fd phage elicited a strong immune response in mice, inducing a high level of circulating RSV-specific antibodies.

Interaction of the viral protein genome linked of turnip mosaic potyvirus with the translational eukaryotic initiation factor (iso) 4E of Arabidopsis thaliana using the yeast two-hybrid system.

The yeast LexA interaction trap was used to screen a cDNA library from Arabidopsis thaliana in order to identify proteins that interact with the viral protein genome linked (VPg)-proteinase of turnip mosaic potyvirus. The screen allowed the isolation of four candidate cDNA clones. Clones pHC4, pHC21, and pHC40 were partially sequenced but no homologies to known proteins were found.

Sources of variation in isolation rate of Giardia lamblia cysts and their homogeneous distribution in river water entering a water treatment plant.

The objective of this work was to determine if differences in the number of Giardia cysts measured in river water were due to the method itself, the analyst, or real differences in the distribution of these cysts in water. To minimize the methodological differences, centrifugation only was used as the primary concentration method. Differences were observed between results from different analysts and they were identified as technical errors.

Subgroup specific protection of mice from respiratory syncytial virus infection with peptides encompassing the amino acid region 174-187 from the G glycoprotein: the role of cysteinyl residues in protection.

We identified subgroup specific protective epitopes represented by the amino acid regions 174-187 and 171-187 of the G glycoproteins from respiratory syncytial virus (RSV), subgroups A and B. Mice immunized with coupled synthetic peptides corresponding to either the region 174-187 containing a Cys186-->Ser substitution or to the native region 171-187 were completely resistant to RSV infection but only to the respective virus. The protective activities of the peptides 174-187 were dependent on the Cys186-->Ser substitution.

Identification and sequence analyses of the granulin gene of Choristoneura fumiferana granulovirus.

The nucleotide sequence of the granulin gene of Choristoneura fumiferana granulovirus (CfGV) was determined. The gene encodes a protein of 248 amino acids with a predicted Mr of 29.299 kDa.

Complete sequences of the neuraminidase genes of swine influenza viruses (H1N1) associated with the respiratory disease in pigs.

The complete nucleotide sequences of neuraminidase (NA) of two swine influenza viruses (H1N1) are presented. A/Sw/Quebec/5393/91 (SwQc91) virus, associated with the chronic respiratory disease and A/Sw/ Quebec/192/81 (SwQc81) virus, associated with the acute respiratory disease, were used. The deduced amino acid sequences of NA of SwQc91 and SwQc81 viruses showed a high degree (>95%) of similarity.

Genomic study of hemagglutinins of swine influenza (H1N1) viruses associated with acute and chronic respiratory diseases in pigs.

The nucleotide sequences of HA1 domain of hemagglutinin of clinical H1N1 influenza viruses, isolated during recent outbreaks of respiratory problems in pig farms of Quebec, was determined. The viruses A/Sw/Quebec/3291/90 (SwQc3291) and A/Sw/Quebec/1747/90 (SwQc1747), associated with chronic respiratory disease, showed close similarity for their deduced aa sequences. When compared with the published data of A/Sw/Quebec/5393/91 (SwQc91), the variations observed included Cb and Ca antigenic sites in SwQc3291 and Sb and Ca sites in SwQc1747 isolates.

Characterization of monoclonal antibodies to the hemagglutinin-esterase glycoprotein of a bovine coronavirus associated with winter dysentery and cross-reactivity to field isolates.

Seven hybridoma cell lines producing monoclonal antibodies (MAbs) to the hemagglutinin-esterase (HE) glycoprotein of bovine coronavirus (BCV) were obtained from BALB/c mice that were immunized with an enriched peplomeric fraction of the winter dysentery (WD)-associated strain BCQ.2590. The specificities of these MAbs to either the dimeric (140-kDa) or the monomeric (65-kDa) form of the HE glycoprotein were determined by Western immunoblotting experiments with purified virus and immunoprecipitation tests with [35S]methionine-labelled infected cell extracts.

Transcriptional and translational expression kinetics of the early gene encoding the BICP27 protein of bovine herpesvirus type 1.

The expression kinetics of an essential trans-regulatory protein, ICP27, from herpes simplex virus type 1 correspond to that of an immediate-early gene whose expression increases rapidly upon infection and then decreases as of 7 hr postinfection. In contrast, here we report that the bovine herpesvirus type 1 (BHV-1) homolog BICP27, a 50-kDa protein, is expressed as an early gene. Both the transcript and protein accumulated gradually reaching peak levels at approximately 12 hr postinfection, after which point steady state levels were maintained up to 24 hr.

Intracellular synthesis, processing, and transport of proteins encoded by ORFs 5 to 7 of porcine reproductive and respiratory syndrome virus.

Porcine Reproductive and Respiratory Syndrome Virus (PRRSV), a small enveloped virus containing a positive-strand RNA genome, possesses at least three major structural proteins designated N, M, and E. The N protein is considered as the major component of the nucleocapsid, whereas M and E are membrane-associated. Previous studies using peptide-specific antibodies assigned these proteins to ORFs 7, 6, and 5, respectively.