Luca Settimo lsettimo at btk.utu.fi
Tue Jan 18 04:10:20 EST 2000

Laurent Terradot wrote:

> Dear Netter,
> I would like to have information about peritrophin. Does anyone know if some
> of these proteins have been described in homopterae insects ?
> Is there some antibodies available ?
> thank you for your help
> best regards,
> Laurent
> Laurent Terradot
> INRA, Station de pathologie végétale
> BP29, 35653 Le Rheu cedex
> terradot at rennes.inra.fr
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Entrez PubMed          1 : Insect Biochem Mol Biol 1999    Related Articles,
Search                 Apr;29(4):319-27                      Books, LinkOut
Help | FAQ                  A peritrophin-like protein expressed in the
                            embryonic tracheae of Drosophila melanogaster.
PubMed Services
Journal Browser             Barry MK, Triplett AA, Christensen AC
MeSH Browser
Single Citation             School of Biological Sciences, University of
Matcher                     Nebraska, Lincoln 68588-0118, USA.
Batch Citation
Matcher                     We have cloned and sequenced a cDNA from
Clinical                    Drosophila melanogaster that encodes a protein
Queries                     homologous to the peritrophins, a family of
                            chitin-binding proteins from the peritrophic
Related                     matrix of insects. Unexpectedly, the gene, Gasp,
Resources                   is expressed in the embryonic tracheae. We
Order Documents             suggest that this family of proteins may be
Grateful Med                present in other tissues than the peritrophic
Consumer Health             matrix, particularly where nutrient or gas
                            exchange are important, and/or where invasion by
                            parasites or viruses is possible. We have also
                            mapped two similar genes that had been sequenced
                            by the Berkeley Drosophila Genome Project, and
                            find that these three very similar genes are not
                            clustered, but are located on three different

                            PMID: 10333571, UI: 99266113


                       2 : J Biol Chem 1998 Jul            Related Articles,
                       10;273(28):17665-70                   Books, Protein,
                                                        Nucleotide, LinkOut
                            A type I peritrophic matrix protein from the
                            malaria vector Anopheles gambiae binds to
                            chitin. Cloning, expression, and

                            Shen Z, Jacobs-Lorena M

                            Case Western Reserve University, School of
                            Medicine, Department of Genetics, Cleveland,
                            Ohio 44106-4955, USA.

                            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.

                            PMID: 9651363, UI: 98316335


                       3 : Insect Biochem Mol Biol 1998    Related Articles,
                       Feb;28(2):99-111                               Books

                            cDNA and deduced amino acid sequences of a
                            peritrophic membrane glycoprotein,
                            'peritrophin-48', from the larvae of Lucilia

                            Schorderet S, Pearson RD, Vuocolo T, Eisemann C,
                            Riding GA, Tellam RL

                            CSIRO Tropical Agriculture, Queensland,

                            The gut of most insects is lined with a
                            semi-permeable peritrophic membrane (or
                            peritrophic matrix) composed of chitin,
                            proteoglycans and proteins. Despite the probable
                            importance of the peritrophic membrane in
                            facilitating the digestive process and
                            protecting insects from invasion by
                            micro-organisms and parasites, there has been
                            little characterization of the specific
                            components and their interactions within this
                            acellular structure. Here we report the
                            characterization of an integral peritrophic
                            membrane glycoprotein, peritrophin-48, from the
                            larvae of the fly Lucilia cuprina, a primary
                            agent of cutaneous myiasis in sheep.
                            Peritrophin-48 was purified from peritrophic
                            membrane obtained by larval culture and its
                            location within the peritrophic membrane
                            determined by immuno-fluorescence and
                            immuno-gold localizations. The cDNA coding for
                            peritrophin-48 was cloned and sequenced. The
                            deduced amino acid sequence codes for a protein
                            of 375 amino acids containing an amino-terminal
                            signal sequence followed by five similar, but
                            non-identical domains, each approximately 65-70
                            amino acids in length and characterised by a
                            specific register of six cysteines. The deduced
                            amino acid sequence shows significant similarity
                            to two other peritrophic membrane proteins,
                            peritrophin-95 and peritrophin-44, from the same
                            species. A reverse transcriptase-PCR approach
                            indicated that there are several highly related
                            peritrophin-48 genes expressed in each
                            individual. Reverse transcriptase-PCR also
                            demonstrated the expression of peritrophin-48 in
                            all three larval instars and adults but not
                            pupae or eggs. Peritrophin-48 was expressed only
                            by the cardia and by the larval midgut. A simple
                            structural model of a basic unit of a type 2
                            peritrophic membrane is presented.

                            PMID: 9639876, UI: 98304029


                       4 : Proc Natl Acad Sci U S A Related Articles, Books,
                       1997 Aug 19;94(17):8939-44       Protein, Nucleotide,
                            Antibody-mediated inhibition of the growth of
                            larvae from an insect causing cutaneous myiasis
                            in a mammalian host.

                            Casu R, Eisemann C, Pearson R, Riding G, East I,
                            Donaldson A, Cadogan L, Tellam R

                            Commonwealth Scientific and Industrial Research
                            Organization (CSIRO) Tropical Agriculture, CSIRO
                            P.M.B. 3, Indooroopilly, 4068 Queensland,

                            Many insects feed on blood or tissue from
                            mammalian hosts. One potential strategy for the
                            control of these insects is to vaccinate the
                            host with antigens derived from the insect. The
                            larvae of the fly Lucilia cuprina feed on ovine
                            tissue and tissue fluids causing a cutaneous
                            myiasis associated with considerable host
                            morbidity and mortality. A candidate vaccine
                            antigen, peritrophin 95, was purified from the
                            peritrophic membrane, which lines the gut of
                            these larvae. Serum from sheep vaccinated with
                            peritrophin 95 inhibited growth of first-instar
                            L. cuprina larvae that fed on this serum. Growth
                            inhibition was probably caused by
                            antibody-mediated blockage of the normally
                            semipermeable peritrophic membrane and the
                            subsequent development of an impervious layer of
                            undefined composition on the gut lumen side of
                            the peritrophic membrane that restricted access
                            of nutrients to the larvae. The amino acid
                            sequence of peritrophin 95 was determined by
                            cloning the DNA complementary to its mRNA. The
                            deduced amino acid sequence codes for a secreted
                            protein containing a distinct Cys-rich domain of
                            317 amino acids followed by a mucin-like domain
                            of 139 amino acids. The Cys-rich domain may be
                            involved in binding chitin. This report
                            describes a novel immunological strategy for the
                            potential control of L. cuprina larvae that may
                            have general application to the control of other
                            insect pests.

                            PMID: 9256413, UI: 97404326


                       5 : J Biol Chem 1996 Apr            Related Articles,
                       12;271(15):8925-35                    Books, Protein,
                                                        Nucleotide, LinkOut
                            Characterization of a major peritrophic membrane
                            protein, peritrophin-44, from the larvae of
                            Lucilia cuprina. cDNA and deduced amino acid

                            Elvin CM, Vuocolo T, Pearson RD, East IJ, Riding
                            GA, Eisemann CH, Tellam RL

                            CSIRO Division of Tropical Animal Production,
                            CSIRO Private Mail Bag 3, Indooroopilly, 4068,
                            Queensland, Australia.

                            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.

                            PMID: 8621536, UI: 96224111


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