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-------------- next part --------------
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Entrez PubMed 1 : Insect Biochem Mol Biol 1999 Related Articles,
Search Apr;29(4):319-27 Books, LinkOut
Overview
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
chromosomes.
PMID: 10333571, UI: 99266113
------------------------------------------------------
2 : J Biol Chem 1998 Jul Related Articles,
10;273(28):17665-70 Books, Protein,
Nucleotide, LinkOut
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A type I peritrophic matrix protein from the
malaria vector Anopheles gambiae binds to
chitin. Cloning, expression, and
characterization.
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
cuprina.
Schorderet S, Pearson RD, Vuocolo T, Eisemann C,
Riding GA, Tellam RL
CSIRO Tropical Agriculture, Queensland,
Australia.
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,
LinkOut
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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,
Australia.
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
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Characterization of a major peritrophic membrane
protein, peritrophin-44, from the larvae of
Lucilia cuprina. cDNA and deduced amino acid
sequences.
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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