The Experts below are selected from a list of 6285 Experts worldwide ranked by ideXlab platform
Lili Chen - One of the best experts on this subject based on the ideXlab platform.
-
penaeus monodon Chitin Binding protein pmcbp is involved in white spot syndrome virus wssv infection
Fish & Shellfish Immunology, 2009Co-Authors: Kuan Yu Chen, Weipang Huang, Tai Ching Hsu, Po Yu Huang, Shih Ting Kang, Lili ChenAbstract:Abstract White spot syndrome virus (WSSV) can cause the most serious viral disease of shrimp and has a wide host range among crustaceans. Although researches show a lot about its genome and structure, information concerning the mechanism of how WSSV infects' cells is lacking. In this study, some experiments were applied to confirm the biological meaning of the protein–protein interaction between WSSV envelope protein, VP53A, and Penaeus monodon Chitin-Binding protein (PmCBP). Immunofluorescent study indicated that PmCBP is located on the cell surface of host cells. PmCBP amounts of about 34 kDa can be detected in both P. monodon and Litopenaeus vannamei tissues by Western blotting. In the in vivo neutralization experiment, both rVP53A and rPmCBP that were produced by Esherichia coli can promote resp. a 40% and 20% survival rate of the shrimp which were challenged by WSSV. Furthermore, a yeast-two-hybrid result revealed that PmCBP could interact with at least 11 WSSV envelope proteins. Those findings suggest that PmCBP may be involved in WSSV infection.
-
white spot syndrome virus envelope protein vp53a interacts with penaeus monodon Chitin Binding protein pmcbp
Diseases of Aquatic Organisms, 2007Co-Authors: Lili Chen, Weipang HuangAbstract:White spot syndrome virus (WSSV) is the causative agent of a severe disease of cultivated shrimp. Using purified WSSV virions, VP53A encoded by open reading frame wssv067 was identified as a structural protein by SDS-PAGE and proteomics. Immunoelectron microscopy with a gold-labeled secondary antibody revealed that VP53A was distributed on the viral envelope. In order to further explore the link between WSSV067 and host proteins, we performed a yeast 2-hybrid screening of a Penaeus monodon cDNA library, using WSSV067C as bait. One of the molecules that specifically interacted with WSSV067C was the P. monodon Chitin-Binding protein (PmCBP). An in vitro Binding assay showed that c-myc-WSSV067C was capable of co-precipitating HA-PmCBP-C. Furthermore, PmCBP was expressed in almost all organs but appeared to be up-regulated at the late stage of WSSV infection.
Ping Wang - One of the best experts on this subject based on the ideXlab platform.
-
magnaporthe oryzae auxiliary activity protein moaa91 functions as Chitin Binding protein to induce appressorium formation on artificial inductive surfaces and suppress plant immunity
Mbio, 2020Co-Authors: Xinyu Liu, Yimei You, Yibin Zou, Muxing Liu, Haifeng Zhang, Xiaobo Zheng, Ping Wang, Yang Wang, Lina Yang, Zhengguang ZhangAbstract:ABSTRACT The appressoria that are generated by the rice blast fungus Magnaporthe oryzae in response to surface cues are important for successful colonization. Previous work showed that regulators of G-protein signaling (RGS) and RGS-like proteins play critical roles in appressorium formation. However, the mechanisms by which these proteins orchestrate surface recognition for appressorium induction remain unclear. Here, we performed comparative transcriptomic studies of ΔMorgs mutant and wild-type strains and found that M. oryzae Aa91 (MoAa91), a homolog of the auxiliary activity family 9 protein (Aa9), was required for surface recognition of M. oryzae. We found that MoAA91 was regulated by the MoMsn2 transcription factor and that its disruption resulted in defects in both appressorium formation on the artificial inductive surface and full virulence of the pathogen. We further showed that MoAa91 was secreted into the apoplast space and was capable of competing with the immune receptor Chitin elicitor-Binding protein precursor (CEBiP) for Chitin Binding, thereby suppressing Chitin-induced plant immune responses. In summary, we have found that MoAa91 is a novel signaling molecule regulated by RGS and RGS-like proteins and that MoAa91 not only governs appressorium development and virulence but also functions as an effector to suppress host immunity. IMPORTANCE The rice blast fungus Magnaporthe oryzae generates infection structure appressoria in response to surface cues largely due to functions of signaling molecules, including G-proteins, regulators of G-protein signaling (RGS), mitogen-activated protein (MAP) kinase pathways, cAMP signaling, and TOR signaling pathways. M. oryzae encodes eight RGS and RGS-like proteins (MoRgs1 to MoRgs8), and MoRgs1, MoRgs3, MoRgs4, and MoRgs7 were found to be particularly important in appressorium development. To explore the mechanisms by which these proteins regulate appressorium development, we have performed a comparative in planta transcriptomic study and identified an auxiliary activity family 9 protein (Aa9) homolog that we named MoAa91. We showed that MoAa91 was secreted from appressoria and that the recombinant MoAa91 could compete with a Chitin elicitor-Binding protein precursor (CEBiP) for Chitin Binding, thereby suppressing Chitin-induced plant immunity. By identifying MoAa91 as a novel signaling molecule functioning in appressorium development and an effector in suppressing host immunity, our studies revealed a novel mechanism by which RGS and RGS-like proteins regulate pathogen-host interactions.
-
analysis of Chitin Binding proteins from manduca sexta provides new insights into evolution of peritrophin a type Chitin Binding domains in insects
Insect Biochemistry and Molecular Biology, 2015Co-Authors: Guillaume Tetreau, Neal T Dittmer, Xiaolong Cao, Sinu Agrawal, Yunru Chen, S Muthukrishnan, Jiang Haobo, Gary W Blissard, Michael R Kanost, Ping WangAbstract:In insects, Chitin is a major structural component of the cuticle and the peritrophic membrane (PM). In nature, Chitin is always associated with proteins among which Chitin-Binding proteins (CBPs) are the most important for forming, maintaining and regulating the functions of these extracellular structures. In this study, a genome-wide search for genes encoding proteins with ChtBD2-type (peritrophin A-type) Chitin-Binding domains (CBDs) was conducted. A total of 53 genes encoding 56 CBPs were identified, including 15 CPAP1s (cuticular proteins analogous to peritrophins with 1 CBD), 11 CPAP3s (CPAPs with 3 CBDs) and 17 PMPs (PM proteins) with a variable number of CBDs, which are structural components of cuticle or of the PM. CBDs were also identified in enzymes of Chitin metabolism including 6 Chitinases and 7 Chitin deacetylases encoded by 6 and 5 genes, respectively. RNA-seq analysis confirmed that PMP and CPAP genes have differential spatial expression patterns. The expression of PMP genes is midgut-specific, while CPAP genes are widely expressed in different cuticle forming tissues. Phylogenetic analysis of CBDs of proteins in insects belonging to different orders revealed that CPAP1s from different species constitute a separate family with 16 different groups, including 6 new groups identified in this study. The CPAP3s are clustered into a separate family of 7 groups present in all insect orders. Altogether, they reveal that duplication events of CBDs in CPAP1s and CPAP3s occurred prior to the evolutionary radiation of insect species. In contrast to the CPAPs, all CBDs from individual PMPs are generally clustered and distinct from other PMPs in the same species in phylogenetic analyses, indicating that the duplication of CBDs in each of these PMPs occurred after divergence of insect species. Phylogenetic analysis of these three CBP families showed that the CBDs in CPAP1s form a clearly separate family, while those found in PMPs and CPAP3s were clustered together in the phylogenetic tree. For Chitinases and Chitin deacetylases, most of phylogenetic analysis performed with the CBD sequences resulted in similar clustering to the one obtained by using catalytic domain sequences alone, suggesting that CBDs were incorporated into these enzymes and evolved in tandem with the catalytic domains before the diversification of different insect orders. Based on these results, the evolution of CBDs in insect CBPs is discussed to provide a new insight into the CBD sequence structure and diversity, and their evolution and expression in insects.
-
a novel Chitin Binding protein identified from the peritrophic membrane of the cabbage looper trichoplusia ni
Insect Biochemistry and Molecular Biology, 2005Co-Authors: Wei Guo, Yi Pang, Ping WangAbstract:A novel midgut peritrophic membrane (PM) protein, TnPM-P42, was identified from the cabbage looper, Trichoplusia ni. TnPM-P42 was shown as a 42kDa protein by SDS-PAGE analysis and appeared to be associated with the PM throughout its entire length. In T. ni larvae, the midgut is the only tissue where TnPM-P42 could be detected during the feeding period of the larvae. TnPM-P42 has Chitin-Binding activity and is strongly associated with the PM, which is similar to the currently known peritrophin type PM proteins. However, TnPM-P42 represents a unique family of proteins distinctly different from the peritrophin type PM proteins in its sequence characteristics. TnPM-P42 does not contain the peritrophin domain which is present in all the currently known PM proteins, but instead has a Chitin deacetylase-like domain. Sequence similarity search of the GenBank database did not result in identification of any known proteins with a significant overall sequence similarity to the TnPM-P42. However, expressed sequence tags (ESTs) from various arthropods were identified to code for proteins with high sequence similarities to TnPM-P42, indicating the presence of TnPM-P42 homologs in other arthropods. Consistent with the identification of various ESTs from arthropods, Western blot analysis demonstrated the presence of a TnPM-P42-like protein in the PMs from Heliothis virescens and Helicoverpa zea larvae. The sequence characteristics of TnPM-P42 indicate that TnPM-P42 represents a novel family of insect proteins. However, its biochemical and physiological functions require further investigation.
-
identification of two new peritrophic membrane proteins from larval trichoplusia ni structural characteristics and their functions in the protease rich insect gut
Insect Biochemistry and Molecular Biology, 2004Co-Authors: Ping Wang, Guoxun Li, Robert R GranadosAbstract:Peritrophic membrane (PM) proteins are important determinants for the structural formation and function of the PM. We identified two new Chitin Binding proteins, named CBP1 and CBP2, from the PM of Trichoplusia ni larvae by cDNA cloning. The proteins contain 12 and 10 tandem Chitin Binding domains in CBP1 and CBP2, respectively. Chitin Binding studies demonstrated the Chitin Binding activity of CBP1 and CBP2, and confirmed the Chitin Binding domain sequence predicted by sequence analysis. Both CBP1 and CBP2 were not mucin-like glycoproteins, however, they were highly resistant to proteolytic degradation by trypsin. We found that in CBP1 and CBP2, potential trypsin and chymotrypsin cleavage sites reside primarily within the Chitin Binding domain sequences, limiting exposure of the potential cleavage sites to the digestive proteinases. This finding suggests a proteinase-resistance mechanism for non-mucin PM proteins to function in the proteinase rich gut environment. Immunohistochemical analysis showed that CBP1 and CBP2 are specifically localized in the PM. However, intact CBP1 and CBP2 proteins were not present in the PM, indicating that their partially degraded fragments were assembled into the PM. This observation suggests that the presence of a large number of Chitin Binding domains in PM proteins allows the proteins to tolerate limited proteolytic degradation in the midgut without loss of their Chitin Binding activity with multiple Chitin Binding domains. Alignment of the Chitin Binding sequences suggested that CBP1 and CBP2 evolved by gene duplication and the tandem Chitin Binding domains in the proteins arose from domain duplications.
Tai Ching Hsu - One of the best experts on this subject based on the ideXlab platform.
-
penaeus monodon Chitin Binding protein pmcbp is involved in white spot syndrome virus wssv infection
Fish & Shellfish Immunology, 2009Co-Authors: Kuan Yu Chen, Weipang Huang, Tai Ching Hsu, Po Yu Huang, Shih Ting Kang, Lili ChenAbstract:Abstract White spot syndrome virus (WSSV) can cause the most serious viral disease of shrimp and has a wide host range among crustaceans. Although researches show a lot about its genome and structure, information concerning the mechanism of how WSSV infects' cells is lacking. In this study, some experiments were applied to confirm the biological meaning of the protein–protein interaction between WSSV envelope protein, VP53A, and Penaeus monodon Chitin-Binding protein (PmCBP). Immunofluorescent study indicated that PmCBP is located on the cell surface of host cells. PmCBP amounts of about 34 kDa can be detected in both P. monodon and Litopenaeus vannamei tissues by Western blotting. In the in vivo neutralization experiment, both rVP53A and rPmCBP that were produced by Esherichia coli can promote resp. a 40% and 20% survival rate of the shrimp which were challenged by WSSV. Furthermore, a yeast-two-hybrid result revealed that PmCBP could interact with at least 11 WSSV envelope proteins. Those findings suggest that PmCBP may be involved in WSSV infection.
Weipang Huang - One of the best experts on this subject based on the ideXlab platform.
-
penaeus monodon Chitin Binding protein pmcbp is involved in white spot syndrome virus wssv infection
Fish & Shellfish Immunology, 2009Co-Authors: Kuan Yu Chen, Weipang Huang, Tai Ching Hsu, Po Yu Huang, Shih Ting Kang, Lili ChenAbstract:Abstract White spot syndrome virus (WSSV) can cause the most serious viral disease of shrimp and has a wide host range among crustaceans. Although researches show a lot about its genome and structure, information concerning the mechanism of how WSSV infects' cells is lacking. In this study, some experiments were applied to confirm the biological meaning of the protein–protein interaction between WSSV envelope protein, VP53A, and Penaeus monodon Chitin-Binding protein (PmCBP). Immunofluorescent study indicated that PmCBP is located on the cell surface of host cells. PmCBP amounts of about 34 kDa can be detected in both P. monodon and Litopenaeus vannamei tissues by Western blotting. In the in vivo neutralization experiment, both rVP53A and rPmCBP that were produced by Esherichia coli can promote resp. a 40% and 20% survival rate of the shrimp which were challenged by WSSV. Furthermore, a yeast-two-hybrid result revealed that PmCBP could interact with at least 11 WSSV envelope proteins. Those findings suggest that PmCBP may be involved in WSSV infection.
-
white spot syndrome virus envelope protein vp53a interacts with penaeus monodon Chitin Binding protein pmcbp
Diseases of Aquatic Organisms, 2007Co-Authors: Lili Chen, Weipang HuangAbstract:White spot syndrome virus (WSSV) is the causative agent of a severe disease of cultivated shrimp. Using purified WSSV virions, VP53A encoded by open reading frame wssv067 was identified as a structural protein by SDS-PAGE and proteomics. Immunoelectron microscopy with a gold-labeled secondary antibody revealed that VP53A was distributed on the viral envelope. In order to further explore the link between WSSV067 and host proteins, we performed a yeast 2-hybrid screening of a Penaeus monodon cDNA library, using WSSV067C as bait. One of the molecules that specifically interacted with WSSV067C was the P. monodon Chitin-Binding protein (PmCBP). An in vitro Binding assay showed that c-myc-WSSV067C was capable of co-precipitating HA-PmCBP-C. Furthermore, PmCBP was expressed in almost all organs but appeared to be up-regulated at the late stage of WSSV infection.
Maurício P. Sales - One of the best experts on this subject based on the ideXlab platform.
-
proteolytic digestive enzymes and peritrophic membranes during the development of plodia interpunctella lepidoptera piralidae targets for the action of soybean trypsin inhibitor sbti and Chitin Binding vicilin evv
Journal of Agricultural and Food Chemistry, 2008Co-Authors: Ticiana M. L. Amorim, Adriana F. Uchoa, Adeliana S. Oliveira, Francisco P. Macedo, Leonardo Lima Pepino De Macedo, Joelma C M Pitanga, Elizeu A Santos, Maurício P. SalesAbstract:The digestive system of P. interpunctella was characterized during its larval development to determine possible targets for the action of proteinaceous enzyme inhibitors and Chitin-Binding proteins. High proteolytic activities using azocasein at pH 9.5 as substrate were found. These specific enzymatic activities (AU/mg protein) showed an increase in the homogenate of third instar larvae, and when analyzed by individual larvae (AU/gut), the increase was in sixth instar larvae. Zymograms showed two bands corresponding to those enzymatic activities, which were inhibited by TLCK and SBTI, indicating that the larvae mainly used serine proteinases at pH 9.5 in their digestive process. The presence of a peritrophic membrane in the larvae was confirmed by chemical testing and light microscopy. In a bioassay, P. interpunctella was not susceptible to the soybean trypsin inhibitor, which did not affect larval mass and mortality, likely due to the weak association with its target digestive enzyme. EvV (Erythrina velutina vicilin), when added to the diet, affected mortality (LD50 0.23%) and larval mass (ED50 0.27%). This effect was associated with EvV-Binding to the peritrophic membrane, as seen by immunolocalization. EvV was susceptible to gut enzymes and after the digestion process, released an immunoreactive fragment that was bound to the peritrophic matrix, which probably was responsible for the action of EvV.
-
Larvicidal Effects of a Chitin-Binding Vicilin from Erythrina velutina Seeds on the Mediterranean Fruit Fly Ceratitis capitata
Journal of agricultural and food chemistry, 2008Co-Authors: Leonardo L. P. Macedo, Ticiana M. L. Amorim, Adriana F. Uchoa, Adeliana S. Oliveira, Jannison K.c. Ribeiro, Francisco P. Macedo, Elizeu Antunes Dos Santos, Maurício P. SalesAbstract:Chitin-Binding vicilin from Erythrina velutina seeds was purified by ammonium sulfate followed by affinity chromatography on a Chitin column and gel filtration on Superose-6-10-300-GL. The Erythrin...
-
effects of a Chitin Binding vicilin from enterolobium contortisiliquum seeds on bean bruchid pests callosobruchus maculatus and zabrotes subfasciatus and phytopathogenic fungi fusarium solani and colletrichum lindemuntianum
Journal of Agricultural and Food Chemistry, 2007Co-Authors: Fabiano T Moura, Leonardo L. P. Macedo, Adeliana S. Oliveira, Elizeu Antunes Dos Santos, Andre L B R Vianna, Lucia B S Andrade, Aparecida S Martinsmiranda, Jose T A Oliveira, Maurício P. SalesAbstract:Chitin-Binding vicilin from Enterolobium contortisiliquum seeds was purified by ammonium sulfate followed by gel filtration on Sephacryl 300-SH and on Sephacryl 200-SH. The vicilin, called EcV, is a dimeric glycoprotein composed of 1.03% carbohydrates and a Mr of 151 kDa, consisting of two subunits of Mr of 66.2 and 63.8 kDa. The EcV homogeneity was confirmed in a PAGE where it was observed to be a unique acid protein band with slow mobility in this native gel. E. contortisiliquum vicilin (EcV) was tested for anti-insect activity against C. maculatus and Zabrotes subfasciatus larvae and for phytopathogenic fungi, F. solani and C. lindemuntianum. EcV was very effective against both bruchids, producing 50% mortality for Z. subfasciatus at an LD50 of 0.43% and affected 50% of the larvae mass with an ED50 of 0.65%. In artificial diets given to C. maculatus, 50% of the larvae mass was affected with an ED50 of 1.03%, and larva mortality was 50% at LD50 of 1.11%. EcV was not digested by midgut homogenates of C. ...