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  • 1
    Publication Date: 2011-02-26
    Description: Metarhizium anisopliae infects mosquitoes through the cuticle and proliferates in the hemolymph. To allow M. anisopliae to combat malaria in mosquitoes with advanced malaria infections, we produced recombinant strains expressing molecules that target sporozoites as they travel through the hemolymph to the salivary glands. Eleven days after a Plasmodium-infected blood meal, mosquitoes were treated with M. anisopliae expressing salivary gland and midgut peptide 1 (SM1), which blocks attachment of sporozoites to salivary glands; a single-chain antibody that agglutinates sporozoites; or scorpine, which is an antimicrobial toxin. These reduced sporozoite counts by 71%, 85%, and 90%, respectively. M. anisopliae expressing scorpine and an [SM1](8):scorpine fusion protein reduced sporozoite counts by 98%, suggesting that Metarhizium-mediated inhibition of Plasmodium development could be a powerful weapon for combating malaria.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4153607/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4153607/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fang, Weiguo -- Vega-Rodriguez, Joel -- Ghosh, Anil K -- Jacobs-Lorena, Marcelo -- Kang, Angray -- St Leger, Raymond J -- 5R21A1079429-02/PHS HHS/ -- R01 AI031478/AI/NIAID NIH HHS/ -- R21 AI079429/AI/NIAID NIH HHS/ -- R21 AI088033/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2011 Feb 25;331(6020):1074-7. doi: 10.1126/science.1199115.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Entomology, University of Maryland, 4112 Plant Sciences Building, College Park, MD 20742, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21350178" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anopheles gambiae/*microbiology/*parasitology/physiology ; Antibodies, Protozoan/immunology ; Base Sequence ; Cloning, Molecular ; Defensins/genetics/metabolism ; Feeding Behavior ; Female ; Hemolymph/metabolism/microbiology/parasitology ; Humans ; Insect Vectors/*microbiology/*parasitology/physiology ; Malaria, Falciparum/transmission ; Metarhizium/*genetics/physiology ; Molecular Sequence Data ; Oligopeptides/genetics/metabolism ; Organisms, Genetically Modified ; Pest Control, Biological ; Plasmodium falciparum/*physiology ; Protozoan Proteins/immunology ; Salivary Glands/metabolism/parasitology ; Spores, Fungal/physiology ; Sporozoites/physiology ; Transformation, Genetic ; Transgenes
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    ISSN: 1432-072X
    Keywords: Chymoelastase ; Trypsin ; Metarhizium anisopliae ; Entomopathogen ; Regulation of synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Synthesis of chymoelastase and trypsin by the entomopathogenic fungus Metarhizium anisopliae occurs rapidly (〈2 h) during carbon and nitrogen derepression in minimal media. Enzyme levels were enhanced when minimal media were supplemented with insect cuticle or other insoluble polymetic nutrients (e.g. cellulose) that were insufficient to produce catabolite repression. Addition of more readily utilized metabolites (e.g. glucose or alanine) repressed protease production confirming that production is constitutive but repressible. Operational control of protease release involves synthesis rather than secretion because catabolite repression reduced endocellular activity (associated with a sedimentable vacuole containing fraction) as well as extracellular enzyme levels. Studies with metabolic inhibitors indicated that production of Pr1 and Pr2 does not require DNA synthesis. However, synthesis is substantially reduced by inhibitors of transcription (actinomycin D and 8-azoguanine) and translation (cyclohexamide and puromycin). Inhibition by 8-azoguanine is relieved by guanine. These results imply that the operative steps in protease regulation involve de novo synthesis of mRNA. Inhibition of enzyme production by an AMP analogue adenosine 5′-0-thiophosphate implies an involvement for AMP-dependent enzyme systems in derepression. However, neither exogenous cAMP nor an inhibitor of cAMP phosphodiesterase relieved catabolite repression by glucose or NH4Cl. Use of o-vanadate to inhibit plasmalemma ATPase confirmed that secretion of chymoelastase-like protease and trypsin-like protease via the cell membrane is an active process.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-0832
    Keywords: Endoprotease ; trypsin ; exoprotease ; aminopeptidase ; entomophthorales ; deuteromycetes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The entomopathogenic entomophthoraceae (zygomycotina) Erynia rhizospora, Erynia dipterigena, and Erynia neoaphidis and the deuteromycete Aspergillus flavus produced single novel endoproteases (pI ca. 9) with activity against trypsin and chymotrypsin substrates. In contrast, the deuteromycete Paecilomyces farinosus produced a chymotrypsin (pI ca. 10). Inhibitor studies confirmed that the mixed activities (purified by isoelectric focusing) were derived from single endoproteases. The most potent inhibitor was Chicken ovoinhibitor. Little or no inhibition was observed for P. farinosus endoprotease by any of the chemicals tested. Although the different fungi possessed a broad spectrum of aminopeptidase activity, 3 species (E. rhizospora, E. dipterigena, and A. flavus) showed a preference for leucine at the N-terminal position and 2 species (E. neoaphidis and P. farinosus) showed maximal activity against arginine. Inhibitor studies confirmed these aminopeptidases as metallo-enzymes.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Entomology 39 (1994), S. 293-322 
    ISSN: 0066-4170
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Type of Medium: Electronic Resource
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