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Two genera of Microsporidia were found infecting mosquito larvae in three localities on the Pacific coast of Choco. Vavraia sp. (Microsporida: Pleistophoridae) was found in larvae of Wyeomyia circumcincta, W. simmsi and Anopheles albimanus collected from plants of the Bromeliacea family in Arusí y Joví. Amblyospora sp. (Microsporida: Amblyosporidae) was found parasitizingAedes angustivittatuslarvae COllectedfrom a terrestrial breeding pond in the locality of Nuqur. Morphology of the spores of the two parasites under light microscopy is described, as well as preliminary data on host range when exposed to laboratory rearad Aedes aegypti, Culex quinquefasciatus and Anopheles albimanus. Their rola in mosquito control is discussed.Se reportan dos géneros de microsporidia que parasitan larvas de mosquitos en criaderos naturales de tres localidades en la costa Pacffica Chocoana. Vavraia sp. (Microsporida: Pleistophoridae) parásita larvas de Wyeomyia circumcincta, de Wyeomya simmsi y de Anopheles neivai, recolectadas en las rosetas de especies de la familia Bromeliaceae en las localidades de Arusí y Joví. Amblyospora sp. (Microsporida: Amblyosporidae) parásita larvas deAedes angustivittatusde criaderos terrestres semipermanentes en la localidad de Nuquí. Se describe la morfología de estos dos microsporidia al microscopio óptico. Estudios preliminares de infección en larvas de Aedes aegypti, Culex quinquefasciatus yAnopheles albimanus, criadas en laboratorio, indican que Vavraia sp. infecta las tres especies, con preferencia a Culex quinquefasciatus. Las larvas expuestas a esporas de Amblyospora sp. no presentaron infección. Se discute el posible papel de estos dos géneros en el control de las poblaciones de mosquitos.

The article presents medical case of a 57-year-old male with hepatitis C and alcohol induced cirrhosis. It states that the patient was presented to the emergency with hemetemesis and hematochezia, followed by lightheadedness and diaphoresis. It also notes that the patient was on warfarin and naproxen following recent knee surgery.

Presents abstract on the article 'Streptococcus Pneumoniae and the Human Nasopharynx.'

Background. Keratins are heteropolymeric proteins that form the intermediate filament cytoskeleton in epithelial cells. The common basic structure of all keratins is organized in a central α-helical rod domain flanked by nonhelical, variable head and tail regions. Most mutations in keratins are found in the central α-helical rod domain. Keratin 9 (K9) is expressed only in the suprabasal layers of palmoplantar epidermis. Mutations in the keratin 9 gene ( KRT9) have been shown to cause epidermolytic palmoplantar keratoderma (EPPK; OMIM 144200), an autosomal dominant genodermatosis characterized clinically by diffuse hyperkeratosis limited to the palms and soles, and histologically by epidermolysis in suprabasal layers of the epidermis. Aim. To elucidate the genetic basis of EPPK in five Pakistani families. Methods. Using microsatellite markers localized to the areas around the type I keratin gene cluster on chromosome 17q21, genotyping of these families was performed, followed by sequencing of the KRT9 gene. Results. The analysis resulted in the identification of two novel (p.M157K and p.Y454H) and two recurrent (p.M157T and p.R163Q) mutations in the KRT9 of all five families. All mutations occurred within the highly conserved helix initiation or termination motif of K9. Conclusions. The affected members of all five families possess mutations in the KRT9 gene that severely affect heterodimer formation with the type II keratin partner. The results of our study further underscore the crucial role of K9 protein in the palmoplantar epidermis. [ABSTRACT FROM AUTHOR]

A letter to the editor is presented on the identification of gene mutation in Pakistani families with hypohidrotic ectodermal dysplasia.

Invasive infection often begins with asymptomatic colonization of mucosal surfaces. A murine model of bacterial colonization with Streptococcus pneumoniae was used to study the mechanism for mucosal protection by immunoglobulin. In previously colonized immune mice, bacteria were rapidly sequestered within large aggregates in the nasal lumen. To further examine the role of bacterial agglutination in protection by specific antibodies, mice were passively immunized with immunoglobulin G (IgG) purified from antipneumococcal sera or pneumococcal type-specific monoclonal human IgA (hIgA1 or hIgA2). Systemically delivered IgG accessed the mucosal surface and blocked acquisition of colonization and transmission between littermates. Optimal protection by IgG was independent of Fc fragment and complement and, therefore, did not involve an opsonophagocytic mechanism. Enzymatic digestion or reduction of IgG before administration showed that protection required divalent binding that maintained its agglutinating effect. Divalent hIgA1 is cleaved by the pneumococcal member of a family of bacterial proteases that generate monovalent Fabα fragments. Thus, passive immunization with hIgA1 blocked colonization by an IgA1-protease-deficient mutant (agglutinated) but not the protease-producing wild-type parent (not agglutinated), whereas protease-resistant hIgA2 agglutinated and blocked colonization by both. Our findings highlight the importance of agglutinating antibodies in mucosal defense and reveal how successful pathogens evade this effect. [ABSTRACT FROM AUTHOR]

Bacterial immunoglobulin A1 (IgA1) proteases may sabotage the protective effects of IgA. In vitro, both exogenous and endogenously produced IgA1 protease inhibited phagocytic killing of Streptococcus pneumoniae by capsule-specific IgA1 human monoclonal antibodies (hMAbs) but not IgA2. These IgA1 proteases cleaved and reduced binding of the the effector Fcα1 heavy chain but not the antigen-binding F(ab)/light chain to pneumococcal surfaces. In vivo, IgA1 protease-resistant IgA2, but not IgA1 protease-sensitive IgA1, supported 60% survival in mice infected with wild-type S. pneumoniae. IgA1 hMAbs protected mice against IgA1 protease-deficient but not -producing pneumococci. Parallel mouse sera with human IgA2 showed more efficient complement-mediated reductions in pneumococci with neutrophils than did IgA1, particularly with protease-producing organisms. After natural human pneumococcal bacteremia, purified serum IgG inhibited IgA1 protease activity in 7 of 11 patients (64%). These observations provide the first evidence in vivo that IgA1 protease can circumvent killing of S. pneumoniae by human IgA. Acquisition of IgA1 protease-neutralizing IgG after infection directs attention to IgA1 protease both as a determinant of successful colonization and infection and as a potential vaccine candidate. [ABSTRACT FROM AUTHOR]

Activation of the CiaRH two-component signaling system prevents the development of competence for genetic transformation in Streptococcus pneumoniae through a previously unknown mechanism. Earlier studies have shown that CiaRH controls the expression of htrA, which we show encodes a surface-expressed serine protease. We found that mutagenesis of the putative catalytic serine of HtrA, while not impacting the competence of a ciaRH+ strain, restored a normal competence profile to a strain having a mutation that constitutively activates the CiaH histidine kinase. This result implies that activity of HtrA is necessary for the CiaRH system to inhibit competence. Consistent with this finding, recombinant HtrA (rHtrA) decreased the competence of pneumococcal cultures. The rHtrA-mediated decline in transformation efficiency could not be corrected with excess competence-stimulating peptide (CSP), suggesting that HtrA does not act through degradation of this signaling molecule. The inhibitory effects of rHtrA and activated CiaH, however, were largely overcome in a strain having constitutive activation of the competence pathway through a mutation in the cytoplasmic domain of the ComD histidine kinase. Although these results suggested that HtrA might act through degradation of the extracellular portion of the Cored receptor, Western immunoblots for ComD did not reveal changes in protein levels attributable to HtrA. We therefore postulate that HtrA may act on an unknown protein target that potentiates the activation of the ComDE system by CSP. These findings suggest a novel regulatory role for pneumococcal HtrA in modulating the activity of a two-component signaling system that controls the development of genetic competence. [ABSTRACT FROM AUTHOR]