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

Elvin, Christopher M.; Vuocolo, Tony; Pearson, Roger; East, I.J.; Riding, George; Eisemann, C.H.; Tellam, Ross L.

doi:10.1074/jbc.271.15.8925

Cited by 172 publications

(141 citation statements)

References 44 publications

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“…5, lanes 2 and 4). Strongly bound PM proteins were also observed in Trichoplusia ni (Lepidoptera) larvae (Wang & Granados 2000) and Lucilia cuprina (Diptera) larvae (Elvin et al 1996). The majority of the total PM proteins from L. cuprina are not solubilized by strong denaturants such as SDS used in our experiments (Tellam et al 1999).…”

Section: Resultsmentioning

confidence: 71%

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Derris (Lonchocarpus) urucu (Leguminosae) Extract Modifies the Peritrophic Matrix Structure of Aedes aegypti (Diptera:Culicidae)

Gusmão

Páscoa

Mathias

et al. 2002

Mem. Inst. Oswaldo Cruz

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Section: Resultsmentioning

confidence: 71%

“…In order to verify whether the D. urucu root bark extract treatment could also interfere in the interaction of PM and its associated proteins, two buffers were sequentially employed to extract PM proteins according to Elvin et al (1996). Ae.…”

Section: Resultsmentioning

confidence: 99%

Derris (Lonchocarpus) urucu (Leguminosae) Extract Modifies the Peritrophic Matrix Structure of Aedes aegypti (Diptera:Culicidae)

Gusmão

Páscoa

Mathias

et al. 2002

Mem. Inst. Oswaldo Cruz

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“…Therefore, we only present one K D for (GlcNAc) 6 , but this K D ITC is only an apparent value. Trp fluorescence quenching experiments have also been reported for peritrophin-44, a CBM14 lectin containing four ChBD repeats (8). In this case, Trp fluorescence quenching was ϳ16% at full saturation for (GlcNAc) 3 , whereas peritrophin-44 only contains one Trp residue in one of the four CBM14 repeats.…”

Section: Table IImentioning

confidence: 58%

Binding of the AVR4 Elicitor of Cladosporium fulvum to Chitotriose Units Is Facilitated by Positive Allosteric Protein-Protein Interactions

Burg

Spronk

Boeren

et al. 2004

Journal of Biological Chemistry

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The attack of fungal cell walls by plant chitinases is an important plant defense response to fungal infection. Anti-fungal activity of plant chitinases is largely restricted to chitinases that contain a noncatalytic, plantspecific chitin-binding domain (ChBD) (also called Hevein domain). Current data confirm that the race-specific elicitor AVR4 of the tomato pathogen Cladosporium fulvum can protect fungi against plant chitinases, which is based on the presence of a novel type of ChBD in AVR4 that was first identified in invertebrates. Although these two classes of ChBDs (Hevein and invertebrate) are sequentially unrelated, they share structural homology. Here, we show that the chitin-binding sites of these two classes of ChBDs have different topologies and characteristics. The K D , ⌬H, and ⌬S values obtained for the interaction between AVR4 and chito-oligomers are comparable with those obtained for Hevein. However, the binding site of AVR4 is larger than that of Hevein, i.e. AVR4 interacts strictly with chitotriose, whereas Hevein can also interact with the monomer N-acetylglucosamine. Moreover, binding of additional AVR4 molecules to chitin occurs through positive cooperative protein-protein interactions. By this mechanism AVR4 is likely to effectively shield chitin on the fungal cell wall, preventing the cell wall from being degraded by plant chitinases.Binding and conversion of carbohydrates by proteins is of fundamental importance in numerous biological processes, including (self and nonself) cell-cell recognition, cell adhesion, and carbohydrate turnover. Recently, protein domains responsible for this interaction have been reclassified into distinct carbohydrate-binding modules (CBMs) 1 (1). CBMs are often present in carbohydrate-degrading enzymes, where they appear to mediate a prolonged and more intimate contact between the catalytic domain and insoluble carbohydrate polymers (2, 3). Lectins, on the other hand, are carbohydratebinding proteins that lack enzymatic activity but often contain tandem repeats of CBMs.Chitin, a polymer consisting of ␤-1,4-linked GlcNAc residues, is a major component of crustacean shells, insect exoskeletons, and fungal cell walls but is absent in plants. In higher organisms, two CBMs predominantly confer binding of proteins to chitin, i.e. the Hevein domain (hereafter denoted as CBM18) (4) and the invertebrate chitin-binding domain (CBM14) (5). CBM18 is nearly exclusively found in plants (to date one additional member of CBM18 has been identified in Streptomyces griseus; Ref. 6), whereas CBM14 is commonly found in the genomes of baculoviridae, invertebrates, and mammals but absent in plants (5). Both ChBDs are typical CBMs, i.e. lectins with tandem repeats are known for both (e.g. wheat germ agglutinin (WGA) (7) and peritrophin-44 (8)), and both domains can be found in chitinases. However, CBM18 is only fused to the plant-specific family 19 catalytic domain, whereas chitinases of mammals and invertebrates utilize CBM14 in combination with the family 18 catalytic domain. Seque...

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“…(14), Penaeus japonica chitinase 1 (Pj-chit1) (27), Chelonus sp. chitinase (Ch-chit) (28), 44-kDa glycoprotein from Lucilia cuprina (Peritrophin-44) (13), and Trichoplusia ni intestinal mucin (Tn-IM) (29). Plants are as follows: hevein from rubber tree (Hevein) (9), Amaranthus caudatus antimicrobial protein 2 (Ac-AMP2) (10), and four homologous domains of wheat germ agglutinin (WGA A, -B, -C, and -D) (11).…”

Section: Nmr Structure Of the Invertebrate Chitin-binding Protein 179mentioning

confidence: 99%

“…It has been well demonstrated that this domain is indispensable for the antimicrobial activity and exhibits a significant conservation in primary sequence (Ͼ40%) and in three-dimensional (3D) 1 structure (9 -12). Although this advanced knowledge has been provided for the plant chitin-binding proteins, less is known for the invertebrate chitin-binding proteins including tachycitin (1,(13)(14)(15)(16). Kawabata et al (1) identified that tachycitin is a 73-residues chitin-binding protein having antimicrobial activity.…”

mentioning

confidence: 99%

Chitin-binding Proteins in Invertebrates and Plants Comprise a Common Chitin-binding Structural Motif

Suetake

Tsuda

Kawabata

et al. 2000

Journal of Biological Chemistry

135

114

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Tachycitin, a 73-residue polypeptide having antimicrobial activity is present in the hemocyte of horseshoe crab (Tachypleus tridentatus). The first three-dimensional structure of invertebrate chitin-binding protein was determined for tachycitin using two-dimensional nuclear magnetic resonance spectroscopy. The measurements indicate that the structure of tachycitin is largely divided into N-and C-terminal domains; the former comprises a three-stranded ␤-sheet and the latter a two-stranded ␤-sheet following a short helical turn. The latter structural motif shares a significant tertiary structural similarity with the chitin-binding domain of plant chitin-binding protein. This result is thought to provide faithful experimental evidence to the recent hypothesis that chitin-binding proteins of invertebrates and plants are correlated by a convergent evolution process.An invertebrate chitin-binding protein named tachycitin is recently found to be a member of the primordial elements of innate immune defense against bacterial and fungal infections (1-5). The antimicrobial activity is initially identified for chitin-binding proteins extracted from plants (6 -7), which commonly comprise single or multiple copies of the chitin-binding domain. The plant chitin-binding domain is mostly composed of 30 -43 residues including eight cysteines, three aromatic residues, and glycines and is frequently referred to as a hevein domain (8). It has been well demonstrated that this domain is indispensable for the antimicrobial activity and exhibits a significant conservation in primary sequence (Ͼ40%) and in three-dimensional (3D) 1 structure (9 -12). Although this advanced knowledge has been provided for the plant chitin-binding proteins, less is known for the invertebrate chitin-binding proteins including tachycitin (1,(13)(14)(15)(16). Kawabata et al. (1) identified that tachycitin is a 73-residues chitin-binding protein having antimicrobial activity. They also revealed that tachycitin consists of five intramolecular disulfide bridges; the connected Cys pairs are 6 -33, 12-30, 24 -61, 25-68, and 40 -53. For invertebrates, the chitin-binding domain was assumed to comprise about 65 residues (17) involving a high percentage of cysteine and aromatic residues in a similar manner to the plant chitin-binding domain. On the basis of such similarity between plant and invertebrate chitin-binding proteins, Shen and Jacobs-Lorena (17) proposed a hypothesis that they are correlated by a rare evolutional process, convergent evolution, i.e. proteins from different origins develop to construct the same active site structure to acquire the same function. However, complete lack of 3D-structural information of invertebrate chitin-binding protein obscures the evolutional relationship between invertebrate and plant chitin-binding proteins. The present study determines the solution structure of tachycitin using NMR spectroscopy, which provides the first 3D structural information of invertebrate chitin-binding protein. EXPERIMENTAL PROCEDURESAn invertebrate...

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

Cited by 172 publications

References 44 publications

Derris (Lonchocarpus) urucu (Leguminosae) Extract Modifies the Peritrophic Matrix Structure of Aedes aegypti (Diptera:Culicidae)

Derris (Lonchocarpus) urucu (Leguminosae) Extract Modifies the Peritrophic Matrix Structure of Aedes aegypti (Diptera:Culicidae)

Binding of the AVR4 Elicitor of Cladosporium fulvum to Chitotriose Units Is Facilitated by Positive Allosteric Protein-Protein Interactions

Chitin-binding Proteins in Invertebrates and Plants Comprise a Common Chitin-binding Structural Motif

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