Evidence map›Paper›PMID 20827401›Full record

ArticleInternational journal of biological sciences2010

Identification and molecular characterization of a new member of the peritrophic membrane proteins from the meadow moth, loxostege sticticalis.

Jiao Yin, Zhao-Jun Wei, Ke-Bin Li, Ya-Zhong Cao, Wei Guo

Abstract read
In one paragraph

Article in International journal of biological sciences, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Jiao YinState Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100193, China.
Zhao-Jun Wei
Ke-Bin Li
Ya-Zhong Cao
Wei Guo

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The peritrophic membrane (PM) plays an important role in protecting insects. The PM proteins are important to determinate the formation and function of the PM. A new PM protein, named Lsti99, was identified from the PM of Loxostege sticticalis larvae by cDNA library screening. The full cDNA of Lsti99 is 1392 bp in length, contains an open reading frame (ORF) of 1245 bp that encodes a preprotein of 415 amino acid residues with a 17-amino acid signal peptide. The sequence of Lsti99 showed no homology to other known PM proteins. The recombinant Lsti99 was successfully expressed in insect cells (Sf9) using recombinant baculoviruses and was used to isolate the antibodies to Lsti99 from the polyclonal antiserum. Lsti99 was expressed mainly in the PM, but weaker bands could be detected in the head and integument as well. The Lsti99 protein could be separated from the PM complex by chitinase in vitro, but M2R did not show effect in vitro confirming the chitin-binding activity of Lsti99. The biochemical and physiological functions of Lsti99 in L. sticticalis require further investigation.

Indexed as

AnimalsBase SequenceChitinasesCloning, MolecularDNA, ComplementaryInsect ProteinsLarvaMembrane ProteinsMolecular Sequence DataMothsRecombinant Fusion ProteinsSequence AlignmentSequence Analysis, DNASequence Analysis, ProteinChitinasesDNA, ComplementaryInsect ProteinsMembrane ProteinsRecombinant Fusion ProteinsChitin-binding activityLoxostege sticticalisLsti99.Peritrophic membrane proteinRecombinant protein

Identifiers

PMID20827401
PMCPMC2935671

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.