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A New Type I Peritrophic Membrane Protein from Larval Holotrichia oblita (Coleoptera: Melolonthidae) Binds to Chitin

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      Abstract

      Peritrophic membranes (PMs) are composed of chitin and protein. Chitin and protein play important roles in the structural formation and function of the PM. A new type I PM protein, HoCBP76, was identified from the Holotrichia oblita. HoCBP76 was shown as a 62.3 kDa protein by SDS-PAGE analysis and appeard to be associated with the PM throughout its entire length. In H. oblita larvae, the midgut is the only tissue where HoCBP76 could be detected during the feeding period of the larvae. The predicted amino acid sequence indicates that it contains seven tandem chitin binding domains belonging to the peritrophin-A family. HoCBP76 has chitin binding activity and is strongly associated with the PM. The HoCBP76 was not a mucin-like glycoprotein, and the consensus of conserved cysteines appeared to be CX 13–17CX 5CX 9CX 12CX 7C. Western blot analysis showed that the abundance of HoCBP76 in the anterior, middle and posterior regions of the midgut was similar, indicating that HoCBP76 was secreted by the whole midgut epithelium, and confirmed the H. oblita PM belonged to the Type I PM. Immunolocalization analysis showed that HoCBP76 was mainly localized in the PM. The HoCBP76 is the first PM protein found in the H. oblita; however, its biochemical and physiological functions require further investigation.

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      Most cited references 33

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      Improved prediction of signal peptides: SignalP 3.0.

      We describe improvements of the currently most popular method for prediction of classically secreted proteins, SignalP. SignalP consists of two different predictors based on neural network and hidden Markov model algorithms, where both components have been updated. Motivated by the idea that the cleavage site position and the amino acid composition of the signal peptide are correlated, new features have been included as input to the neural network. This addition, combined with a thorough error-correction of a new data set, have improved the performance of the predictor significantly over SignalP version 2. In version 3, correctness of the cleavage site predictions has increased notably for all three organism groups, eukaryotes, Gram-negative and Gram-positive bacteria. The accuracy of cleavage site prediction has increased in the range 6-17% over the previous version, whereas the signal peptide discrimination improvement is mainly due to the elimination of false-positive predictions, as well as the introduction of a new discrimination score for the neural network. The new method has been benchmarked against other available methods. Predictions can be made at the publicly available web server
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        Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence.

        Post-translational modifications (PTMs) occur on almost all proteins analyzed to date. The function of a modified protein is often strongly affected by these modifications and therefore increased knowledge about the potential PTMs of a target protein may increase our understanding of the molecular processes in which it takes part. High-throughput methods for the identification of PTMs are being developed, in particular within the fields of proteomics and mass spectrometry. However, these methods are still in their early stages, and it is indeed advantageous to cut down on the number of experimental steps by integrating computational approaches into the validation procedures. Many advanced methods for the prediction of PTMs exist and many are made publicly available. We describe our experiences with the development of prediction methods for phosphorylation and glycosylation sites and the development of PTM-specific databases. In addition, we discuss novel ideas for PTM visualization (exemplified by kinase landscapes) and improvements for prediction specificity (by using ESS--evolutionary stable sites). As an example, we present a new method for kinase-specific prediction of phosphorylation sites, NetPhosK, which extends our earlier and more general tool, NetPhos. The new server, NetPhosK, is made publicly available at the URL http://www.cbs.dtu.dk/services/NetPhosK/. The issues of underestimation, over-prediction and strategies for improving prediction specificity are also discussed.
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          Peritrophic matrix structure and function.

          Formed of proteins, glycoproteins, and chitin microfibrils in a proteoglycan matrix, the peritrophic matrix (PM) separates the food from the midgut epithelium in most but not all insects. A PM occurs in two forms. A type I PM is delaminated from the entire midgut epithelium and, in some cases, may only be formed in response to feeding and the type of meal ingested. A type II PM is produced by a specialized region of the anterior midgut called the cardia and forms a continuous sleeve (or sleeves) that is always present. As it is positioned between food and midgut epithelium, the PM plays key roles in the intestinal biology of the insect. The PM may protect the midgut epithelium from mechanical damage and insult from pathogens and toxins; it must act as a semipermeable membrane regulating passage of molecules between the different midgut compartments; and it may separate the midgut lumen into different, physiologically significant compartments.
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            Author and article information

            Affiliations
            [1 ]Institute of Cereal and Oil Crops, Hebei Academy of Agriculture and Forestry Sciences, Shijiazhuang 050035, Hebei, China; E-Mail: xiaominliu1981@ 123456gmail.com
            [2 ]Plant Science and Technology College, Beijing University of Agriculture, Beijing 102206, China
            [3 ]College of Plant Protection, Agricultural University of Hebei/Biological Control Centre of Plant Pathogens and Plant Pests of Hebei Province, Baoding 071001, Hebei, China; E-Mails: liruijun@ 123456163.com (R.L.); zhaodan@ 123456163.com (D.Z.); yjihn@ 123456163.com (X.L.)
            [4 ]Shijiazhuang Development and Reform Commission, Shijiazhuang 050011, Hebei, China; E-Mail: lijie@ 123456163.com
            Author notes

            Author Contributions

            Conceived and designed the experiments: WG. Performed the experiments: XML, JL, DZ, XNL. Analyzed the data: XML, RJL. Wrote the paper: XML, WG.

            [* ]Author to whom correspondence should be addressed; E-Mail: guowei@ 123456hebau.edu.cn ; Tel./Fax: +86-312-7528-178.
            Journal
            Int J Mol Sci
            Int J Mol Sci
            ijms
            International Journal of Molecular Sciences
            Molecular Diversity Preservation International (MDPI)
            1422-0067
            April 2014
            22 April 2014
            : 15
            : 4
            : 6831-6842
            24758927 4013664 10.3390/ijms15046831 ijms-15-06831
            © 2014 by the authors; licensee MDPI, Basel, Switzerland

            This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

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