Anopheles albimanus

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Mario H Rodriguez - One of the best experts on this subject based on the ideXlab platform.

  • Ecdysis-related pleiotropic neuropeptides expression during Anopheles albimanus development.
    Salud Publica De Mexico, 2017
    Co-Authors: Alejandro Alvarado-delgado, Ken Moran-francia, Guillermo Perales-ortiz, Mario H Rodriguez, Humberto Lanz-mendoza
    Abstract:

    Abstract: Objective: To analyze the transcription pattern of neuropeptides in the ontogeny of a malaria vector, the mosquito Anopheles albimanus. Materials and methods: The transcription pattern of Crustacean CardioActive peptide (CCAP), corazonin, Ecdysis Triggering Hormone (ETH), allatostatin-A, orcokinin, Insulin Like Peptide 2 (ILP2), Insulin Like Peptide 5 (ILP5) and bursicon was evaluated using qPCR on larvae (1st - 4th instar), pupae and adult mosquitoes. Results: Unlike in other insects, transcripts of CCAP (70.8%), ETH (60.2%) and corazonin (76.5%) were expressed in 4th instar larvae, probably because these three neuropeptides are associated with the beginning of ecdysis. The neuropeptide ILP2 showed higher transcription levels in other stages and orcokinin decreased during the development of the mosquito. Conclusion: The CCAP, corazonin and ETH neuropeptides are potential targets for the design of control strategies aimed at disrupting An. albiamnus larval development.

  • An antibody against an Anopheles albimanus midgut myosin reduces Plasmodium berghei oocyst development
    Parasites & vectors, 2016
    Co-Authors: Alba N. Lecona-valera, Mario H Rodriguez, Rhoel R. Dinglasan, Dingyin Tao, Tomás López, Maria Del Carmen Rodriguez
    Abstract:

    Background Malaria parasites are transmitted by Anopheles mosquitoes. Although several studies have identified mosquito midgut surface proteins that are putatively important for Plasmodium ookinete invasion, only a few have characterized these protein targets and demonstrated transmission-blocking activity. Molecular information about these proteins is essential for the development of transmission-blocking vaccines (TBV). The aim of the present study was to test three monoclonal antibodies (mAbs), A-140, A-78 and A-10, for their ability to recognize antigens and block oocyst infection of the midgut of Anopheles albimanus, a major malaria vector in Latin America.

  • Antimicrobial properties of Anopheles albimanus pericardial cells.
    Cell and tissue research, 2012
    Co-Authors: Salvador Hernández-martínez, Humberto Lanz-mendoza, Jesús Martínez-barnetche, Mario H Rodriguez
    Abstract:

    Insect pericardial cells (PCs) are strategically located along the dorsal vessel where they encounter a high hemolymph flow enabling them to undertake their osmoregulatory, detoxifying, and scavenging functions. In this location, PCs also encounter foreign molecules and microorganisms. The response of PCs of the mosquito Anopheles albimanus, one of the most important Plasmodium vivax vectors in Mexico and Latin America, to Saccharomyces cerevisiae was analyzed by using biochemical, cellular, ultrastructural, and bioinformatics approaches. Immune gene transcripts were identified in the PC transcriptome of A. albimanus. PCs responded to the presence of yeast and zymosan with increased lysosomal and phosphatase activities and produced lytic activity against bacteria. Our results indicate that mosquito PCs play a key role in the neutralization and elimination of pathogens.

  • GP35 ANOAL, an abundant acidic glycoprotein of female Anopheles albimanus saliva.
    Insect molecular biology, 2007
    Co-Authors: Febe Elena Cázares-raga, Jesús Martínez-barnetche, Lilia González-cerón, Mónica González-lázaro, C. Montero‐solis, Fernando Z. Zamudio, Jorge Aurelio Torres-monzón, M. Ovilla‐muñoz, Javier Aguilar-fuentes, Mario H Rodriguez
    Abstract:

    Salivary glands of female mosquitoes produce proteins, not completely described yet, that participate in carbohydrate and blood feeding. Here, we report an acidic glycoprotein of 35 kDa (GP35 ANOAL) secreted in the saliva of the malaria vector mosquito Anopheles albimanus . GP35 ANOAL is produced exclusively in the distal lateral lobes of adult female salivary glands, it has a pI of 4.45 and is negatively stained by regular silver stain. An 888 bp cDNA clone encoding a predicted product of 240 amino acids has a signal peptide, potential post-translational modification sites, and a disintegrin signature RGD. The GP35 ANOAL sequence depicts high similarities with the 30 kDa saliva allergen of Aedes aegypti , 30 kDa allergen-like hypothetical proteins, and GE-rich proteins present in several Anopheles species, as well as in Ae. albopictus and Culex pipiens quinquefasciatus . The function of this protein family is still unknown.

  • Phormidium animalis (Cyanobacteria: Oscillatoriaceae) supports larval development of Anopheles albimanus.
    Journal of the American Mosquito Control Association, 2003
    Co-Authors: M. Guadalupe Vazquez-martinez, Mario H Rodriguez, Juan I. Arredondo-jimenez, José D. Mendez-sanchez
    Abstract:

    The capability of Phormidium animalis, a cyanobacterium commonly found in larval habitats of Anopheles albimanus in southern Mexico, to support lar val development of this mosquito was investigated. First-stage larvae were reared under insectary conditions with P. animalis ad libitum and their development was compared with larvae fed with wheat germ The time of pupation and adult mosquito size, assessed by wing length, were similar in both aroups, but fewer adult mosquitoes were obtained from larvae fed with the cyanobacteria. Nevertheless, these observations indicate that P. animalis is ingested and assimilated by larval An. albimanus, making this cyanobacterium a good candidate for generic engineering for the introduction of mosquitocidal toxins for malaria control in the region.

José M. C. Ribeiro - One of the best experts on this subject based on the ideXlab platform.

  • NAD(P)H-dependent production of oxygen reactive species by the salivary glands of the mosquito Anopheles albimanus
    Insect biochemistry and molecular biology, 1996
    Co-Authors: José M. C. Ribeiro
    Abstract:

    Salivary gland homogenates of the adult female mosquito Anopheles albimanus, but not those of Aedes aegypti, induced light production in the presence of NADPH and luminol, indicating a NADPH oxidase activity producing reactive oxygen species (superoxide anion) by the anopheline salivary homogenate. Superoxide production by the anopheline salivary homogenate was also confirmed by the NADPH-dependent, superoxide dismutase inhibitable, reduction of cytochrome c. The NADPH oxidase reaction measured by light production in the presence of luminol was inhibited by superoxide dismutase and catalase. Both NADH and NADPH were substrates for the production of oxygen reactive species by the salivary homogenate. Activity, as measured by luminol-dependent light emission, was enhanced one order of magnitude in the presence of 1.6 mg/ml of either phosphatidylserine or bovine serum albumin. Molecular sieving and hydroxyapatite chromatography of the salivary homogenate showed coelution of the NADPH oxidase activity with the previously reported salivary peroxidase activity. It is suggested that the salivary peroxidase of Anopheles albimanus has the ability of producing superoxide in the presence of NADPH, and this may provide the peroxidase with substrates necessary for peroxidation of vasoconstrictor amines such as serotonin, released by aggregating platelets at the site of mosquito probing and feeding.

  • the salivary catechol oxidase peroxidase activities of the mosquito Anopheles albimanus
    The Journal of Experimental Biology, 1993
    Co-Authors: José M. C. Ribeiro, Roberto H. Nussenzveig
    Abstract:

    Salivary gland homogenates from adult female Anopheles albimanus mosquitoes relaxed aortic rings preconstricted with noradrenaline (NA). This relaxation is slow and is due to destruction of NA. Incubation of NA with the homogenate yielded a product with a spectrum consistent with the corresponding adrenochrome. Oxidation of NA was enhanced by a superoxide generation system and inhibited by the combined action of superoxide dismutase and catalase. Additionally, peroxidase activity on both synthetic (o-dianisidine) and biologically active (serotonin) substrates was also present in the salivary gland homogenates, this latter activity requiring hydrogen peroxide. Noradrenaline oxidation, serotonin and o-dianisidine peroxidation and vasodilation all co-elute with a heme protein of relative molecular mass 50,000, as determined by molecular sieving chromatography. Peroxidase activity was localized in the posterior (female-specific) lobes of salivary glands and was also detected in nitrocellulose membranes probed by hungry mosquitoes. Protein and peroxidase activities were significantly lower in salivary glands of mosquitoes after probing and feeding on blood. It is suggested that adult female Anopheles albimanus mosquitoes contain a salivary heme peroxidase that functions during blood finding and blood feeding by destroying hemostatically active biogenic amines released by the vertebrate host during tissue destruction.

  • The salivary catechol oxidase/peroxidase activities of the mosquito Anopheles albimanus
    The Journal of experimental biology, 1993
    Co-Authors: José M. C. Ribeiro, Roberto H. Nussenzveig
    Abstract:

    Salivary gland homogenates from adult female Anopheles albimanus mosquitoes relaxed aortic rings preconstricted with noradrenaline (NA). This relaxation is slow and is due to destruction of NA. Incubation of NA with the homogenate yielded a product with a spectrum consistent with the corresponding adrenochrome. Oxidation of NA was enhanced by a superoxide generation system and inhibited by the combined action of superoxide dismutase and catalase. Additionally, peroxidase activity on both synthetic (o-dianisidine) and biologically active (serotonin) substrates was also present in the salivary gland homogenates, this latter activity requiring hydrogen peroxide. Noradrenaline oxidation, serotonin and o-dianisidine peroxidation and vasodilation all co-elute with a heme protein of relative molecular mass 50,000, as determined by molecular sieving chromatography. Peroxidase activity was localized in the posterior (female-specific) lobes of salivary glands and was also detected in nitrocellulose membranes probed by hungry mosquitoes. Protein and peroxidase activities were significantly lower in salivary glands of mosquitoes after probing and feeding on blood. It is suggested that adult female Anopheles albimanus mosquitoes contain a salivary heme peroxidase that functions during blood finding and blood feeding by destroying hemostatically active biogenic amines released by the vertebrate host during tissue destruction.

Roberto H. Nussenzveig - One of the best experts on this subject based on the ideXlab platform.

  • the salivary catechol oxidase peroxidase activities of the mosquito Anopheles albimanus
    The Journal of Experimental Biology, 1993
    Co-Authors: José M. C. Ribeiro, Roberto H. Nussenzveig
    Abstract:

    Salivary gland homogenates from adult female Anopheles albimanus mosquitoes relaxed aortic rings preconstricted with noradrenaline (NA). This relaxation is slow and is due to destruction of NA. Incubation of NA with the homogenate yielded a product with a spectrum consistent with the corresponding adrenochrome. Oxidation of NA was enhanced by a superoxide generation system and inhibited by the combined action of superoxide dismutase and catalase. Additionally, peroxidase activity on both synthetic (o-dianisidine) and biologically active (serotonin) substrates was also present in the salivary gland homogenates, this latter activity requiring hydrogen peroxide. Noradrenaline oxidation, serotonin and o-dianisidine peroxidation and vasodilation all co-elute with a heme protein of relative molecular mass 50,000, as determined by molecular sieving chromatography. Peroxidase activity was localized in the posterior (female-specific) lobes of salivary glands and was also detected in nitrocellulose membranes probed by hungry mosquitoes. Protein and peroxidase activities were significantly lower in salivary glands of mosquitoes after probing and feeding on blood. It is suggested that adult female Anopheles albimanus mosquitoes contain a salivary heme peroxidase that functions during blood finding and blood feeding by destroying hemostatically active biogenic amines released by the vertebrate host during tissue destruction.

  • The salivary catechol oxidase/peroxidase activities of the mosquito Anopheles albimanus
    The Journal of experimental biology, 1993
    Co-Authors: José M. C. Ribeiro, Roberto H. Nussenzveig
    Abstract:

    Salivary gland homogenates from adult female Anopheles albimanus mosquitoes relaxed aortic rings preconstricted with noradrenaline (NA). This relaxation is slow and is due to destruction of NA. Incubation of NA with the homogenate yielded a product with a spectrum consistent with the corresponding adrenochrome. Oxidation of NA was enhanced by a superoxide generation system and inhibited by the combined action of superoxide dismutase and catalase. Additionally, peroxidase activity on both synthetic (o-dianisidine) and biologically active (serotonin) substrates was also present in the salivary gland homogenates, this latter activity requiring hydrogen peroxide. Noradrenaline oxidation, serotonin and o-dianisidine peroxidation and vasodilation all co-elute with a heme protein of relative molecular mass 50,000, as determined by molecular sieving chromatography. Peroxidase activity was localized in the posterior (female-specific) lobes of salivary glands and was also detected in nitrocellulose membranes probed by hungry mosquitoes. Protein and peroxidase activities were significantly lower in salivary glands of mosquitoes after probing and feeding on blood. It is suggested that adult female Anopheles albimanus mosquitoes contain a salivary heme peroxidase that functions during blood finding and blood feeding by destroying hemostatically active biogenic amines released by the vertebrate host during tissue destruction.

Adolfo Martínez-palomo - One of the best experts on this subject based on the ideXlab platform.

  • Scanning Electron Microscopy of Egg Hatching of Anopheles albimanus (Diptera: Culicidae)
    Journal of medical entomology, 1992
    Co-Authors: Mario H Rodriguez, Arnoldo Orozco, Bibiana Chavez, Adolfo Martínez-palomo
    Abstract:

    Scanning electron and light microscopic observations showed that egg hatching in Anopheles albimanus Wiedemann is aided by a chisel-shaped spine. This hatching tooth is surrounded by a thin flexible membrane fixed to a groove in the head of the larvae. Increased intracranial pressure may force the spine against the egg shell until a fissure is produced. Further opening of the egg is achieved by movements of the head and the entire body of the larva.

  • Scanning electron microscopic observations of Anopheles albimanus (Diptera: Culicidae) eggs.
    Journal of medical entomology, 1992
    Co-Authors: Mario H Rodriguez, Arnoldo Orozco, Bibiana Chavez, Enrique Loyola, Adolfo Martínez-palomo
    Abstract:

    To investigate the existence of subspecies of Anopheles albimanus Wiedeman in southern Mexico, the egg morphology of specimens obtained from several field populations and from insectary-adapted colonies of uniform pupal phenotype was examined. Scanning electron microscopic observations have shown that the eggs of An. albimanus are polymorphic in respect to the size and shape of their floats, but not in their ornamentation. Four types of eggs were found. Differences in the proportion of the various morphological types were statistically significant, although proportions of egg types were variable among individuals within the same population. These observations are suggestive of distinctive populations and warrant further studies using more sensitive methods to investigate sibling species in An. albimanus sensu lato.

Margarita M. Correa - One of the best experts on this subject based on the ideXlab platform.