Lucilia cuprina: Inhibition of larval growth induced by immunization of host sheep with extracts of larval peritrophic membrane

East, I.J.; Fitzgerald, C. J.; Pearson, Roger; Donaldson, R. A.; Vuocolo, Tony; Cadogan, L. C.; Tellam, Ross L.; Eisemann, C.H.

doi:10.1016/0020-7519(93)90144-n

Cited by 63 publications

(34 citation statements)

References 21 publications

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“…This knowledge could be used to develop novel strategies to control malaria transmission. For instance, the blood of sheep vaccinated with the L. cuprina larval PM (type 2) hinders larval development, probably because of the blockage of PM pores (32,33). Although the adult mosquito forms a different type of PM (type 1), it is conceivable that antibodies to adult Anopheles PM proteins will have a similar effect on the PM.…”

Section: Discussionmentioning

confidence: 99%

A Type I Peritrophic Matrix Protein from the Malaria VectorAnopheles gambiae Binds to Chitin

Shen

Jacobs-Lorena

1998

Journal of Biological Chemistry

161

127

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Upon feeding, mosquito midguts secrete the peritrophic matrix (PM), an extracellular chitin-containing envelope that completely surrounds the blood meal. Because the malaria parasite must cross the PM to complete its life cycle in the mosquito, the PM is a potential barrier for malaria transmission. By antibody screening of an expression library we have identified and partially characterized a cDNA encoding a putative PM protein, termed Anopheles gambiae adult peritrophin 1 (Ag-Aper1). Ag-Aper1 is the first cloned PM gene from a disease vector. Northern analysis detected an abundant Ag-Aper1 transcript only in the adult gut, and not in any other tissues or at any other stages of development. The predicted amino acid sequence indicates that it has two tandem chitin-binding domains that share high sequence similarity with each other and also with the chitin-binding domain of an adult gut-specific chitinase from the same organism. The presumed ability of Ag-Aper1 to bind chitin was verified by a functional assay with the baculovirus-expressed recombinant protein. Ag-Aper1 did bind to chitin but not to cellulose, indicating that Ag-Aper1 binds chitin specifically. The double chitin-binding domain organization of Ag-Aper1 suggests that each protein molecule is able to link two chitin polymer chains. Hence, this protein is likely to act as a molecular linker that connects PM chitin fibrils into a three-dimensional network.

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Section: Discussionmentioning

confidence: 99%

A Type I Peritrophic Matrix Protein from the Malaria VectorAnopheles gambiae Binds to Chitin

Shen

Jacobs-Lorena

1998

Journal of Biological Chemistry

161

127

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“…Preparation of Peritrophin-44-The laboratory culture of L. cuprina larvae and harvesting of PM from these larvae have been described elsewhere (12,16). The PM (dry weight, 1 g) was obtained from 320,000 larvae cultured in vitro in 20 batches and was stored at Ϫ70°C in PBS (20 mM Na 2 PO 4 /140 mM NaCl, pH 7.2) containing 2.5 mM benzamidine and 5 mM EDTA.…”

Section: Methodsmentioning

confidence: 99%

“…Blots-Protein samples were analyzed by SDS-polyacrylamide gel electrophoresis (PAGE) and lectin blots according to previously described procedures (12,17). The M r of PM proteins separated by SDS-PAGE were measured by interpolation of a plot of log molecular weight of the standard proteins against their relative mobility.…”

Section: Sds-polyacrylamide Gel Electrophoresis and Lectinmentioning

confidence: 99%

“…Disruption of the functions of these integral PM proteins by chemical or immunological means could lead to novel mechanisms of insect control. Indeed, it is possible to vaccinate sheep against the tissue-and blood-feeding larvae of the fly Lucilia cuprina using isolated PM proteins (12,14). It was demonstrated that antibodies to a PM protein, peritrophin-44, inhibited the free movement of small 6 nm gold particles from the gut lumen across the PM to the underlying digestive epithelial cells.…”

mentioning

confidence: 99%

“…A subset of these proteins is the strongly bound or integral PM proteins, which can only be released from the PM by strong denaturants (12). These latter proteins, which we have named "peritrophins," are probably of central importance for the maintenance of the structural and protective biological functions of the PM and may be involved in determining the ultrafilter character of the membrane (13).…”

mentioning

confidence: 99%

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Characterization of a Major Peritrophic Membrane Protein, Peritrophin-44, from the Larvae of Lucilia cuprina

Elvin

Vuocolo

Pearson

et al. 1996

Journal of Biological Chemistry

172

131

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The peritrophic membrane is a semi-permeable chitinous matrix lining the gut of most insects and is thought to have important roles in the maintenance of insect gut structure, facilitation of digestion, and protection from invasion by microrganisms and parasites. Proteins are integral components of this matrix, although the structures and functions of these proteins have not been characterized in any detail. The peritrophic membrane from the larvae of the fly Lucilia cuprina, the primary agent of cutaneous myiasis in sheep, was shown to contain six major integral peritrophic membrane proteins. Two of these proteins, a 44-kDa glycoprotein (peritrophin-44) and a 48-kDa protein (peritrophin-48) together represent >70% of the total mass of the integral peritrophic membrane proteins. Peritrophin-44 was purified and its complete amino acid sequence was determined by cloning and sequencing the DNA complementary to its mRNA. The deduced amino acid sequence codes for a protein of 356 amino acids containing an amino-terminal signal sequence followed by five similar but nonidentical domains, each of approximately 70 amino acids and characterized by a specific register of 6 cysteines. One of these domains was also present in the noncatalytic regions of chitinases from Brugia malayi, Manduca sexta, and Chelonus. Peritrophin-44 has a uniform distribution throughout the larval peritrophic membrane. Reverse transcriptase-polymerase chain reaction detected the expression of peritrophin-44 in all three larval instars but only trace levels in adult L. cuprina. The protein binds specifically to tri-N-acetyl chitotriose and reacetylated chitosan in vitro. It is concluded that the multiple cysteine-rich domains in peritrophin-44 are responsible for binding to chitin, the major constituent of peritrophic membrane. Peritrophin-44 probably has roles in the maintenance of peritrophic membrane structure and in the determination of the porosity of the peritrophic membrane. This report represents the first characterization of an insect peritrophic membrane protein.

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Secretion of the type 2 peritrophic matrix protein, peritrophin‐15, from the cardia

Eisemann

Wijffels

Tellam

2001

Arch Insect Biochem Physiol

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The midgut of most insects is lined with a peritrophic matrix, which is thought to facilitate digestion and protect the midgut digestive epithelial cells from abrasive damage and invasion by ingested micro-organisms. The type 2 peritrophic matrix is synthesised by a complex and highly specialised organ called the cardia typically located at the junction of the cuticle-lined foregut and midgut. Although the complex anatomy of this small organ has been described, virtually nothing is known of the molecular processes that lead to the assembly of the type 2 peritrophic matrix in the cardia. As a step towards understanding the synthesis of the peritrophic matrix, the synthesis and secretion of the intrinsic peritrophic matrix protein, peritrophin-15 has been followed in the cardia of Lucilia cuprina larvae using immuno-gold localisations. The protein is synthesised by cardia epithelial cells, which have abundant rough endoplasmic reticulum, Golgi, and vesicles indicative of a general secretory function. Peritrophin-15 is packaged into secretory vesicles probably produced from Golgi and transported to the cytoplasmic face of the apical plasma membrane. The vesicles fuse with the plasma membrane at the base of the microvilli and release peritrophin-15 into the inter-microvilli spaces. The protein then becomes associated with the nascent peritrophic matrix, which lies along the tips of the epithelial cell microvilli. It is proposed that peritrophin-15 binds to the ends of chitin fibrils present in the nascent peritrophic matrix, thereby protecting the fibril from the action of exochitinases.

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Lucilia cuprina: Inhibition of larval growth induced by immunization of host sheep with extracts of larval peritrophic membrane

Cited by 63 publications

References 21 publications

A Type I Peritrophic Matrix Protein from the Malaria VectorAnopheles gambiae Binds to Chitin

A Type I Peritrophic Matrix Protein from the Malaria VectorAnopheles gambiae Binds to Chitin

Characterization of a Major Peritrophic Membrane Protein, Peritrophin-44, from the Larvae of Lucilia cuprina

Secretion of the type 2 peritrophic matrix protein, peritrophin‐15, from the cardia

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