Phlebotomus papatasi and Leishmania major parasites express α-amylase and α-glucosidase

Jacobson, Raymond L.; Schlein, Yosef

doi:10.1016/s0001-706x(00)00164-9

Cited by 31 publications

(28 citation statements)

References 27 publications

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“…The expression of both genes might be further influenced by feeding. Differentially regulated a-amylase paralogs were described in Aedes aegypti, in which one gene was reported to be tissue specific for the salivary gland (Grossman and James, 1993), or in Phlebotomus papatasi, in which the transcript of one paralog was upregulated in the midgut after plant feeding (Jacobson and Schlein, 2001). Stauffer et al (1992) described several alleles of a-amylase as products of a single AmyI gene.…”

Section: Discussionmentioning

confidence: 99%

“…Its enzymatic activity was detected in the salivary glands and guts of various insect species and seems to have distinct regulation in both tissues (Grossman et al, 1997;Charlab et al, 1999;Jacobson and Schlein, 2001). The genes encoding a-amylase are often duplicated and may even form a multigene family comprising up to seven members in some species (Kikkawa, 1953;Ogita, 1968;Levy et al, 1985;Pope et al, 1986;Da Lage et al, 2002;Zhang et al, 2003;Sugino, 2007).…”

Section: Introductionmentioning

confidence: 99%

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Characterization of two closely related α‐amylase paralogs in the bark beetle, Ips typographus (L.)

Viktorinová

Kučerová

Bohmova

et al. 2011

Arch Insect Biochem Physiol

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Ips typographus (L.), the eight-spined spruce bark beetle, causes severe damage throughout Eurasian spruce forests and suitable nuclear markers are needed in order to study its population structure on a genetic level. Two closely related genes encoding a-amylase in I. typographus were characterized and named AmyA and AmyB. Both a-amylase paralogs consisted of six exons and five introns. AmyA encodes a polypeptide of 483 amino acids, whereas AmyB has two alternative transcripts encoding polypeptides of 483 and 370 amino acids. The expression levels of both genes were high during larval stage and adulthood. The AmyB transcripts were absent in the pupal stage. A modification of the allozyme staining method allowed us to detect two clusters of bands on the electrophoretic gel that may correspond to the two a-amylase genes. There was a correlation between the lack of AmyB expression in pupa and the absence of the fast migrating isozyme cluster at this stage, suggesting that the faster migrating isoforms are products of the AmyB gene, whereas the slowly migrating bands are derived from the AmyA. C 2011 Wiley Periodicals, Inc.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Characterization of two closely related α‐amylase paralogs in the bark beetle, Ips typographus (L.)

Viktorinová

Kučerová

Bohmova

et al. 2011

Arch Insect Biochem Physiol

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“…These differences may be due to several factors, such as the amount and composition of the food ingested, preference for a specific vertebrate host, behavior or feeding habits of the different species (7,(47)(48)(49)(50), and are factors that can play mitigating roles in L. ovallesi and L. migonei vectorial capacity. These differences may have co-evolved among the different sand fly salivary proteins and the host in order (1) to avoid homeostasis of the vertebrate host and (2) to ease the ingestion by presenting specific activities such as coagulation cascade inhibition, platelet aggregation and vasodilatation.…”

Section: Resultsmentioning

confidence: 99%

Las glándulas salivales de dos flebotominos vectores de Leishmania: Lutzomyia migonei (França) y Lutzomyia ovallesi (Ortiz) (Diptera: Psychodidae)

et al. 2010

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Introduction. Leishmaniasis is a vector-borne disease transmitted by the intradermal inoculation of Leishmania (Kinetoplastida: Trypanosomatidae) promastigotes together with saliva during the bite of an infected sand fly. Objective. The salivary glands were compared from two vector species, Lutzomyia ovallesi (Ortiz,1952) and Lutzomyia migonei (França,1920) (Diptera: Psychodidae). Material and methods. Protein profiles by SDS PAGE of salivary glands were compared among species as well as their development at several times post feeding. First, mice were immunized to salivary proteins by exposure to biting by L. ovallesi and of L. migonei. Antibodies in these mice against salivary gland-specific proteins were evaluated by immunoblotting. Results. No apparent change was revealed in the kinetic expression of salivary proteins induced by the different physiological states post feeding. Qualitative and quantitative variations were detected in16-18 polypeptides with molecular weights ranging from 6 to 180 kDa. Species-specific proteins were demonstrated for L. migonei and L. ovallesi. In addition, antibodies against salivary gland specific proteins were found in mice immunized by the saliva of both species. Conclusion. Basic information was obtained concerning the nature of salivary gland proteins of L. migonei and L. ovallesi. This information helps to elucidate the role of salivary proteins and their potential as effective tools in screening risk factors in human and other vertebrate hosts.

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“…The growth of L. major promastigotes was similar in media supplemented with either 4.5 g/l starch or 25 mM glucose, but in media without any supplement, exponential growth was signi®cantly lower during the logphase and was 40% lower at the stationary phase [10].…”

Section: A-amylase and A-glucosidasementioning

confidence: 92%

“…a-Glucosidase activity increased in guts of both sexes and in the salivary glands of the females (Fig. 1) [10].…”

Section: A-amylase and A-glucosidasementioning

confidence: 94%

The biological function of sand fly and Leishmania glycosidases

Schlein

2001

Med Microbiol Immunol

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This is a summary of the recent work on some glycosidases of sand flies and their Leishmania parasites. Glycosidases catalyze the hydrolysis of complex sugar subunits of polysaccharides into simple sugars. Leishmania major parasites secrete chitinase and N-acetylglucosaminase, which enables them to survive in the gut of the sand fly and are important in facilitating their transmission by the phlebotomine sand fly Phlebotomus papatasi. These enzymes are found in a wide range of trypanosomatids and the gene locus is highly conserved. The sand flies feed on plants and the ingested tissues may contain cellulose particles that the sand flies are unable to digest. Cellulolytic enzymes are secreted by L. major promastigotes and this may help to break down cellulose in infected flies and sustain their growth. Starch is a main photosynthesis product that is stored in leaves. Starch grains have been found in the midguts of field caught sand flies and alpha-amylase, the specific enzyme for starch, has been found in the salivary glands and other organs of Lutzomyia longipalpis and P. papatasi. Alpha-amylase and alpha-glucosidase are expressed by L. major promastigotes and alpha-glucosidase is secreted by several trypanosomatid genera, but not by all those examined. Primers originally designed to amplify P. papatasi amylase DNA sequences, by polymerase chain reaction (PCR), also amplified DNA from all Old World Leishmania species, indicating that the gene is highly conserved between sand flies and these parasites.

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Phlebotomus papatasi and Leishmania major parasites express α-amylase and α-glucosidase

Cited by 31 publications

References 27 publications

Characterization of two closely related α‐amylase paralogs in the bark beetle, Ips typographus (L.)

Characterization of two closely related α‐amylase paralogs in the bark beetle, Ips typographus (L.)

Las glándulas salivales de dos flebotominos vectores de Leishmania: Lutzomyia migonei (França) y Lutzomyia ovallesi (Ortiz) (Diptera: Psychodidae)

The biological function of sand fly and Leishmania glycosidases

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