المؤلفون: Klionsky, DJ, Abdelmohsen, K, Abe, A, Abedin, MJ, Abeliovich, H, Arozena, AA, Adachi, H, Adams, CM, Adams, PD, Adeli, K, Adhihetty, PJ, Adler, SG, Agam, G, Agarwal, R, Aghi, MK, Agnello, M, Agostinis, P, Aguilar, PV, Aguirre-Ghiso, J, Airoldi, EM, Ait-Si-Ali, S, Akematsu, T, Akporiaye, ET, Al-Rubeai, M, Albaiceta, GM, Albanese, C, Albani, D, Albert, ML, Aldudo, J, Algul, H, Alirezaei, M, Alloza, I, Almasan, A, Almonte-Beceril, M, Alnemri, ES, Alonso, C, Altan-Bonnet, N, Altieri, DC, Alvarez, S, Alvarez-Erviti, L, Alves, S, Amadoro, G, Amano, A, Amantini, C, Ambrosio, S, Amelio, I, Amer, AO, Amessou, M, Amon, A, An, ZY, Anania, FA, Andersen, SU, Andley, UP, Andreadi, CK, Andrieu-Abadie, N, Anel, A, Ann, DK, Anoopkumar-Dukie, S, Antonioli, M, Aoki, H, Apostolova, N, Aquila, S, Aquilano, K, Araki, K, Arama, E, Aranda, A, Araya, J, Arcaro, A, Arias, E, Arimoto, H, Ariosa, AR, Armstrong, JL, Arnould, T, Arsov, I, Asanuma, K, Askanas, V, Asselin, E, Atarashi, R, Atherton, SS, Atkin, JD, Attardi, LD, Auberger, P, Auburger, G, Aurelian, L, Autelli, R, Avagliano, L, Avantaggiati, ML, Avrahami, L, Awale, S, Azad, N, Bachetti, T, Backer, JM, Bae, DH, Bae, JS, Bae, ON, Bae, SH, Baehrecke, EH, Baek, SH, Baghdiguian, S, Bagniewska-Zadworna, A, Bai, H, Bai, J, Bai, XY, Bailly, Y, Balaji, KN, Balduini, W, Ballabio, A, Balzan, R, Banerjee, R, Banhegyi, G, Bao, HJ, Barbeau, B, Barrachina, MD, Barreiro, E, Bartel, B, Bartolome, A, Bassham, DC, Bassi, MT, Bast, RC, Basu, A, Batista, MT, Batoko, H, Battino, M, Bauckman, K, Baumgarner, BL, Bayer, KU, Beale, R, Beaulieu, JF, Beck, GR, Becker, C, Beckham, JD, Bedard, PA, Bednarski, PJ, Begley, TJ, Behl, C, Behrends, C, Behrens, GMN, Behrns, KE, Bejarano, E, Belaid, A, Belleudi, F, Benard, G, Berchem, G, Bergamaschi, D, Bergami, M, Berkhout, B, Berliocchi, L, Bernard, A, Bernard, M, Bernassola, F, Bertolotti, A, Bess, AS, Besteiro, S, Bettuzzi, S, Bhalla, S, Bhattacharyya, S, Bhutia, SK, Biagosch, C, Bianchi, MW, Biard-Piechaczyk, M, Billes, V, Bincoletto, C, Bingol, B, Bird, SW, Bitoun, M, Bjedov, I, Blackstone, C, Blanc, L, Blanco, GA, Blomhoff, HK, Boada-Romero, E, Bockler, S, Boes, M, Boesze-Battaglia, K, Boise, LH, Bolino, A, Boman, A, Bonaldo, P, Bordi, M, Bosch, J, Botana, LM, Botti, J, Bou, G, Bouche, M, Bouchecareilh, M, Boucher, MJ, Boulton, ME, Bouret, SG, Boya, P, Boyer-Guittaut, M, Bozhkov, PV, Brady, N, Braga, VMM, Brancolini, C, Braus, GH, Bravo-San Pedro, JM, Brennan, LA, Bresnick, EH, Brest, P, Bridges, D, Bringer, MA, Brini, M, Brito, GC, Brodin, B, Brookes, PS, Brown, EJ, Brown, K, Broxmeyer, HE, Bruhat, A, Brum, PC, Brumell, JH, Brunetti-Pierri, N, Bryson-Richardson, RJ, Buch, S, Buchan, AM, Budak, H, Bulavin, DV, Bultman, SJ, Bultynck, G, Bumbasirevic, V, Burelle, Y, Burke, RE, Burmeister, M, Butikofer, P, Caberlotto, L, Cadwell, K, Cahova, M, Cai, DS, Cai, JJ, Cai, Q, Calatayud, S, Camougrand, N, Campanella, M, Campbell, GR, Campbell, M, Campello, S, Candau, R, Caniggia, I, Cantoni, L, Cao, LZ, Caplan, AB, Caraglia, M, Cardinali, C, Cardoso, SM, Carew, JS, Carleton, LA, Carlin, CR, Carloni, S, Carlsson, SR, Carmona-Gutierrez, D, Carneiro, LAM, Carnevali, O, Carra, S, Carrier, A, Carroll, B, Casas, C, Casas, J, Cassinelli, G, Castets, P, Castro-Obregon, S, Cavallini, G, Ceccherini, I, Cecconi, F, Cederbaum, AI, Cena, V, Cenci, S, Cerella, C, Cervia, D, Cetrullo, S, Chaachouay, H, Chae, HJ, Chagin, AS, Chai, CY, Chakrabarti, G, Chamilos, G, Chan, EYW, Chan, MTV, Chandra, D, Chandra, P, Chang, CP, Chang, RCC, Chang, TY, Chatham, JC, Chatterjee, S, Chauhan, S, Che, YS, Cheetham, ME, Cheluvappa, R, Chen, CJ, Chen, G, Chen, GC, Chen, GQ, Chen, HZ, Chen, JW, Chen, JK, Chen, M, Chen, MZ, Chen, PW, Chen, Q, Chen, SD, Chen, S, Chen, SSL, Chen, W, Chen, WJ, Chen, WQ, Chen, WL, Chen, XM, Chen, YH, Chen, YG, Chen, Y, Chen, YY, Chen, YS, Chen, YJ, Chen, YQ, Chen, Z, Cheng, A, Cheng, CHK, Cheng, H, Cheong, HS, Cherry, S, Chesney, J, Cheung, CHA, Chevet, E, Chi, HC, Chi, SG, Chiacchiera, F, Chiang, HL, Chiarelli, R, Chiariello, M, Chieppa, M, Chin, LS, Chiong, M, Chiu, GNC, Cho, DH, Cho, SG, Cho, WC, Cho, YY, Cho, YS, Choi, AMK, Choi, EJ, Choi, EK, Choi, JY, Choi, ME, Choi, SI, Chou, TF, Chouaib, S, Choubey, D, Choubey, V, Chow, KC, Chowdhury, K, Chu, CT, Chuang, TH, Chun, T, Chung, HW, Chung, TJ, Chung, YL, Chwae, YJ, Cianfanelli, V, Ciarcia, R, Ciechomska, IA, Ciriolo, MR, Cirone, M, Claerhout, S, Clague, MJ, Claria, J, Clarke, PGH, Clarke, R, Clementi, E, Cleyrat, C, Cnop, M, Coccia, EM, Cocco, T, Codogno, P, Coers, J, Cohen, EEW, Colecchia, D, Coletto, L, Coll, NS, Colucci-Guyon, E, Comincini, S, Condello, M, Cook, KL, Coombs, GH, Cooper, CD, Cooper, JM, Coppens, I, Corasaniti, MT, Corazzari, M, Corbalan, R, Corcelle-Termeau, E, Cordero, MD, Corral-Ramos, C, Corti, O, Cossarizza, A, Costelli, P, Costes, S, Coto-Montes, A, Cottet, S, Couve, E, Covey, LR, Cowart, LA, Cox, JS, Coxon, FP, Coyne, CB, Cragg, MS, Craven, RJ, Crepaldi, T, Crespo, JL, 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Diaz-Meco, MT, Diaz-Nido, J, Dickey, CA, Dickson, RC, Diederich, M, Digard, P, Dikic, I, Dinesh-Kumar, SP, Ding, C, Ding, WX, Ding, ZF, Dini, L, Distler, JHW, Diwan, A, Djavaheri-Mergny, M, Dmytruk, K, Dobson, RCJ, Doetsch, V, Dokladny, K, Dokudovskaya, S, Donadelli, M, Dong, XC, Dong, XN, Dong, Z, Donohue, TM, Doran, KS, D'Orazi, G, Dorn, GW, Dosenko, V, Dridi, S, Drucker, L, Du, J, Du, LL, Du, LH, du Toit, A, Dua, P, Duan, L, Duann, P, Dubey, VK, Duchen, MR, Duchosal, MA, Duez, H, Dugail, I, Dumit, VI, Duncan, MC, Dunlop, EA, Dunn, WA, Dupont, N, Dupuis, L, Duran, RV, Durcan, TM, Duvezin-Caubet, S, Duvvuri, U, Eapen, V, Ebrahimi-Fakhari, D, Echard, A, Eckhart, L, Edelstein, CL, Edinger, AL, Eichinger, L, Eisenberg, T, Eisenberg-Lerner, A, Eissa, NT, El-Deiry, WS, El-Khoury, V, Elazar, Z, Eldar-Finkelman, H, Elliott, CJH, Emanuele, E, Emmenegger, U, Engedal, N, Engelbrecht, AM, Engelender, S, Enserink, JM, Erdmann, R, Erenpreisa, J, Eri, R, Eriksen, JL, Erman, A, Escalante, R, Eskelinen, EL, Espert, L, Esteban-Martinez, L, Evans, TJ, Fabri, M, Fabrias, G, Fabrizi, C, Facchiano, A, Faergeman, NJ, Faggioni, A, Fairlie, WD, Fan, CH, Fan, DP, Fan, J, Fang, SY, Fanto, M, Fanzani, A, Farkas, T, Faure, M, Favier, FB, Fearnhead, H, Federici, M, Fei, E, Felizardo, TC, Feng, H, Feng, YB, Feng, YC, Ferguson, TA, Fernandez, AF, Fernandez-Barrena, MG, Fernandez-Checa, JC, Fernandez-Lopez, A, Fernandez-Zapico, ME, Feron, O, Ferraro, E, Ferreira-Halder, CV, Fesus, L, Feuer, R, Fiesel, FC, Filippi-Chiela, EC, Filomeni, G, Fimia, GM, Fingert, JH, Finkbeiner, S, Finkel, T, Fiorito, F, Fisher, PB, Flajolet, M, Flamigni, F, Florey, O, Florio, S, Floto, RA, Folini, M, Follo, C, Fon, EA, Fornai, F, Fortunato, F, Fraldi, A, Franco, R, Francois, A, Frankel, LB, Fraser, IDC, Frey, N, Freyssenet, DG, Frezza, C, Friedman, SL, Frigo, DE, Fu, DX, Fuentes, JM, Fueyo, J, Fujitani, Y, Fujiwara, Y, Fujiya, M, Fukuda, M, Fulda, S, Fusco, C, Gabryel, B, Gaestel, M, Gailly, P, Gajewska, M, 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Zois, CE, Zoladek, T, Zong, WX, Zorzano, A, Zughaier, SM

المصدر: Autophagy. 12(1):1-222

مصطلحات موضوعية: Medicin och hälsovetenskap

الوصول الحر: http://kipublications.ki.se/Default.aspx?queryparsed=id:133288356Test

المؤلفون: Panagi, I, Jennings, E, Zeng, J, Günster, RA, Stones, CD, Mak, H, Jin, E, Stapels, DAC, Subari, NZ, Pham, THM, Brewer, SM, Ong, SYQ, Monack, DM, Helaine, S, Thurston, TLM

المساهمون: Medical Research Council (MRC), Lister Institute of Preventive Medicine, Biotechnology and Biological Sciences Research Council (BBSRC)

المصدر: 53.e6 ; 41

مصطلحات موضوعية: GSK3, M2, SPI2, STAT3, Salmonella, SteE, dual-specificity kinases, host-pathogen interactions, macrophage polarization, Immunology, 0605 Microbiology, 1108 Medical Microbiology

جغرافية الموضوع: United States

الوصف: Many Gram-negative bacterial pathogens antagonize anti-bacterial immunity through translocated effector proteins that inhibit pro-inflammatory signaling. In addition, the intracellular pathogen Salmonella enterica serovar Typhimurium initiates an anti-inflammatory transcriptional response in macrophages through its effector protein SteE. However, the target(s) and molecular mechanism of SteE remain unknown. Here, we demonstrate that SteE converts both the amino acid and substrate specificity of the host pleiotropic serine/threonine kinase GSK3. SteE itself is a substrate of GSK3, and phosphorylation of SteE is required for its activity. Remarkably, phosphorylated SteE then forces GSK3 to phosphorylate the non-canonical substrate signal transducer and activator of transcription 3 (STAT3) on tyrosine-705. This results in STAT3 activation, which along with GSK3 is required for SteE-mediated upregulation of the anti-inflammatory M2 macrophage marker interleukin-4Rα (IL-4Rα). Overall, the conversion of GSK3 to a tyrosine-directed kinase represents a tightly regulated event that enables a bacterial virulence protein to reprogram innate immune signaling and establish an anti-inflammatory environment.

العلاقة: Cell Host and Microbe; http://hdl.handle.net/10044/1/76008Test; MR/M009629/1; n/a; BB/R011834/1

الإتاحة: https://doi.org/10.1016/j.chom.2019.11.002Test
http://hdl.handle.net/10044/1/76008Test

المؤلفون: Jennings, E, Esposito, D, Rittinger, K, Thurston, TLM

المساهمون: Wellcome Trust

المصدر: 15329 ; 15316

مصطلحات موضوعية: Science & Technology, Life Sciences & Biomedicine, Biochemistry & Molecular Biology, Salmonella enterica, bacterial pathogenesis, metalloprotease, type III secretion system (T3SS), NF-B, substrate specificity, bacterial effectors, GtgA, virulence factor, KAPPA-B, SECRETION SYSTEM, SUBSTRATE RECOGNITION, ESCHERICHIA-COLI, DNA, HOMODIMER, NLEC, MECHANISM, SPECIFICITY, REFINEMENT, NF-κB

الوصف: The closely related type III secretion system zinc metalloprotease effector proteins GtgA, GogA, and PipA are translocated into host cells during Salmonella infection. They then cleave nuclear factor κ-light-chain-enhancer of activated B cells (NF-κB) transcription factor subunits, dampening activation of the NF-κB signaling pathway and thereby suppressing host immune responses. We demonstrate here that GtgA, GogA, and PipA cleave a subset of NF-κB subunits, including p65, RelB, and cRel but not NF-κB1 and NF-κB2, whereas the functionally similar type III secretion system effector NleC of enteropathogenic and enterohemorrhagic Escherichia coli cleaved all five NF-κB subunits. Mutational analysis of NF-κB subunits revealed that a single nonconserved residue in NF-κB1 and NF-κB2 that corresponds to the P1′ residue Arg-41 in p65 prevents cleavage of these subunits by GtgA, GogA, and PipA, explaining the observed substrate specificity of these enzymes. Crystal structures of GtgA in its apo-form and in complex with the p65 N-terminal domain explained the importance of the P1′ residue. Furthermore, the pattern of interactions suggested that GtgA recognizes NF-κB subunits by mimicking the shape and negative charge of the DNA phosphate backbone. Moreover, structure-based mutational analysis of GtgA uncovered amino acids that are required for the interaction of GtgA with p65, as well as those that are required for full activity of GtgA in suppressing NF-κB activation. This study therefore provides detailed and critical insight into the mechanism of substrate recognition by this family of proteins important for bacterial virulence.

العلاقة: Journal of Biological Chemistry; http://hdl.handle.net/10044/1/63545Test; https://dx.doi.org/10.1074/jbc.RA118.004255Test

الإتاحة: https://doi.org/10.1074/jbc.RA118.004255Test
http://hdl.handle.net/10044/1/63545Test

المؤلفون: Bourgeois, JS, Zhou, D, Thurston, TLM, Gilchrist, JJ, Ko, DC

المساهمون: Wellcome Trust

مصطلحات موضوعية: Science & Technology, Life Sciences & Biomedicine, Immunology, Infectious Diseases, SPI-1, Salmonella, flagellar motility, inflammation, metJ, metabolism, methionine salvage, methylthioadenosine, virulence regulation, ENTERICA SEROVAR TYPHIMURIUM, STATE ANALOG INHIBITORS, SAH/MTA NUCLEOSIDASE INHIBITORS, STRUCTURE-BASED DESIGN, ESCHERICHIA-COLI, GENE-EXPRESSION, INVASION GENES, 5'-METHYLTHIOADENOSINE PHOSPHORYLASE, ANTIMICROBIAL ACTIVITY, MACROPHAGE APOPTOSIS, 06 Biological Sciences, 11 Medical And Health Sciences, 07 Agricultural And Veterinary Sciences, Microbiology

جغرافية الموضوع: United States

الوصف: In order to deploy virulence factors at appropriate times and locations, microbes must rapidly sense and respond to various metabolite signals. Previously we showed transient elevation of the methionine-derived metabolite methylthioadenosine (MTA) in serum during systemic Salmonella enterica serovar Typhimurium (S. Typhimurium) infection. Here we explored the functional consequences of increased MTA concentrations on S. Typhimurium virulence. We found that MTA-but not other related metabolites involved in polyamine synthesis and methionine salvage-reduced motility, host cell pyroptosis, and cellular invasion. Further, we developed a genetic model of increased bacterial endogenous MTA production by knocking out the master repressor of the methionine regulon, metJ Like MTA-treated S. Typhimurium, the ΔmetJ mutant displayed reduced motility, host cell pyroptosis, and invasion. These phenotypic effects of MTA correlated with suppression of flagellar and Salmonella pathogenicity island-1 (SPI-1) networks. ΔmetJ S. Typhimurium had reduced virulence in oral and intraperitoneal infection of C57BL/6J mice, independently of the effects of MTA on SPI-1. Finally, ΔmetJ bacteria induced a less severe inflammatory cytokine response in a mouse sepsis model. Together, these data indicate that exposure of S. Typhimurium to MTA or disruption of the bacterial methionine metabolism pathway suppresses S. Typhimurium virulence.

العلاقة: Infection and Immunity; http://hdl.handle.net/10044/1/62765Test; https://dx.doi.org/10.1128/IAI.00429-18Test; 097816/Z/11/B

الإتاحة: https://doi.org/10.1128/IAI.00429-18Test
http://hdl.handle.net/10044/1/62765Test

المؤلفون: Boyle, KB, Thurston, TLM, Randow, F

المصدر: 2509 ; 2508

مصطلحات موضوعية: Science & Technology, Life Sciences & Biomedicine, Cell Biology, antibacterial autophagy, NDP52, optineurin, PI(3)P, Salmonella, TBK1, WIPI, Animals, Humans, Models, Biological, Nuclear Proteins, Protein-Serine-Threonine Kinases, Salmonella typhimurium, Vacuoles, 0601 Biochemistry And Cell Biology, Biochemistry & Molecular Biology

الوصف: Defense of the mammalian cell cytosol against Salmonella invasion is reliant upon capture of the infiltrating bacteria by macroautophagy (hereafter autophagy), a process controlled by the kinase TBK1. In our recent study we showed that recruitment of TBK1 activity to Salmonella stabilizes the key autophagy regulator WIPI2 on those bacteria, a novel and essential function for TBK1 in the control of the early steps of antibacterial autophagy. Substantial redundancy exists in the precise recruitment mechanism for TBK1 because engagement with any of several Salmonella-associated ‘eat-me’ signals, including host-derived glycans, and K48- and K63-linked ubiquitin chains, suffices to recruit TBK1 functionality. We therefore propose that buffering TBK1 recruitment against potential bacterial interference might be of evolutionary advantage to the host.

العلاقة: Autophagy; http://hdl.handle.net/10044/1/58057Test; https://dx.doi.org/10.1080/15548627.2016.1235126Test

الإتاحة: https://doi.org/10.1080/15548627.2016.1235126Test
http://hdl.handle.net/10044/1/58057Test

المؤلفون: Esposito, D, Günster, RA, Martino, L, El Omari, K, Wagner, A, Thurston, TLM, Rittinger, K

المساهمون: Wellcome Trust

المصدر: 5078 ; 5064

مصطلحات موضوعية: Science & Technology, Life Sciences & Biomedicine, Biochemistry & Molecular Biology, glycosyltransferase, Salmonella enterica, protein structure, enzyme mechanism, bacterial toxin, X-ray crystallography, arginine modification, bacterial effectors, glycosyltransferase type-A, SseK3, UDP-GlcNAc, GT-A family, structural analysis, CLOSTRIDIUM-DIFFICILE TOXIN, III SECRETION SYSTEM, CONFORMATIONAL-CHANGES, ESCHERICHIA-COLI, DEATH DOMAIN, GLUCOSYLTRANSFERASE ACTIVITY, CRYSTAL-STRUCTURE, PROTEIN, HOST, GLCNACYLATION, arginine-modification, glycosyltransgerase type-A

جغرافية الموضوع: United States

الوصف: The Salmonella secreted effector SseK3 translocates into host cells, targeting innate immune responses including NF-κB activation. SseK3 is a glycosyltransferase that transfers an N-acetylglucosamine (GlcNAc) moiety onto the guanidino group of a target arginine, modulating host cell function. However, a lack of structural information has precluded elucidation of the molecular mechanisms in arginine and GlcNAc selection. We report here the crystal structure of SseK3 in its apo form and in complex with hydrolysed UDP-GlcNAc. SseK3 possesses the typical glycosyltransferase type-A (GT-A)-family fold and the metal-coordinating DXD motif essential for ligand binding and enzymatic activity. Several conserved residues were essential for arginine-GlcNAcylation and SseK3-mediated inhibition of NF-κB activation. Isothermal titration calorimetry revealed SseK3's preference for manganese coordination. The pattern of interactions in the substrate-bound SseK3 structure explained the selection of the primary ligand. Structural re-arrangement of the C-terminal residues upon ligand binding was crucial for SseK3's catalytic activity and NMR analysis indicated that SseK3 has limited UDP-GlcNAc hydrolysis activity. The release of free N-acetyl α-D-glucosamine, and the presence of the same molecule in the SseK3 active site, classified it as a retaining glycosyltransferase. A glutamate residue in the active site suggested a double-inversion mechanism for the arginine N-glycosylation reaction. Homology models of SseK1, SseK2, and the Escherichia coli orthologue NleB1, reveal differences in the surface electrostatic charge distribution possibly accounting for their diverse activities. This first structure of a retaining GT-A arginine N-glycosyltransferase provides an important step towards a better understanding of this enzyme class and their roles as bacterial effectors.

العلاقة: Journal of Biological Chemistry; http://hdl.handle.net/10044/1/57972Test; https://dx.doi.org/10.1074/jbc.RA118.001796Test; 097816/Z/11/B

الإتاحة: https://doi.org/10.1074/jbc.RA118.001796Test
http://hdl.handle.net/10044/1/57972Test

المؤلفون: James J. Gilchrist, Thurston Tlm, Jeffrey S. Bourgeois, Daoguo Zhou, Koa Dc

مصطلحات موضوعية: 0303 health sciences, Methionine, 030306 microbiology, Pyroptosis, Virulence, Motility, Biology, biology.organism_classification, Microbiology, 03 medical and health sciences, chemistry.chemical_compound, Regulon, chemistry, Salmonella enterica, Genetic model, bacteria, Pathogen, 030304 developmental biology

الوصف: In order to deploy virulence factors at appropriate times and locations, microbes must rapidly sense and respond to various metabolite signals. Previously we showed transient elevation of the methionine-derived metabolite methylthioadenosine (MTA) in serum during systemicSalmonella entericaserovar Typhimurium (S.Typhimurium) infection. Here we explored the functional consequences of increased MTA concentrations onS.Typhimurium virulence. We found that MTA—but not other related metabolites involved in polyamine synthesis and methionine salvage—reduced motility, host cell pyroptosis, and cellular invasion. Further, we developed a genetic model of increased bacterial endogenous MTA production by knocking out the master repressor of the methionine regulon,metJ. Like MTA treatedS.Typhimurium, the ΔmetJmutant displayed reduced motility, host cell pyroptosis, and invasion. These phenotypic effects of MTA correlated with suppression of flagellar andSalmonellapathogenicity island-1 (SPI-1) networks. ΔmetJ S.Typhimurium had reduced virulence in oral infection of C57BL/6 mice. Finally, ΔmetJbacteria induced a less severe inflammatory cytokine response in a mouse sepsis model. These data provide a possible bacterial mechanism for our previous findings that pretreating mice with MTA dampens inflammation and prolongs survival. Together, these data indicate that exposure ofS.Typhimurium to MTA or disruption of the bacterial methionine metabolism pathway is sufficient to suppress SPI-1 mediated processes, motility, andin vivovirulence.SignificanceSalmonella entericaserovar Typhimurium (S. Typhimurium) is a leading cause of gastroenteritis and bacteremia worldwide. Widespread multi-drug resistance, inadequate diagnostics, and the absence of a vaccine for use in humans, all contribute to the global burden of morbidity and mortality associated withS.Typhimurium infection. Here we find that increasing the concentration of the methionine derived metabolite methylthioadenosine, either inS.Typhimurium or in its environment, is sufficient to suppress virulence processes. These findings could be leveraged to inform future therapeutic interventions againstS.Typhimurium aimed at manipulating either host or pathogen methylthioadenosine production.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03bf7f984b0927945c7ed13c105fd997Test

المؤلفون: Gunster, RA, Matthews, SA, Holden, DW, Thurston, TLM

مصطلحات موضوعية: Science & Technology, Life Sciences & Biomedicine, Immunology, Infectious Diseases, 06 Biological Sciences, 11 Medical And Health Sciences, 07 Agricultural And Veterinary Sciences, Microbiology

العلاقة: Infection and Immunity; http://hdl.handle.net/10044/1/52451Test; https://dx.doi.org/10.1128/IAI.00242-17Test

الإتاحة: https://doi.org/10.1128/IAI.00242-17Test
http://hdl.handle.net/10044/1/52451Test

المؤلفون: Thurston, TLM, Wandel, MP, Von Muhlinen, N, Foeglein, A, Randow, F

المصدر: 418 ; 414

مصطلحات موضوعية: Science & Technology, Multidisciplinary Sciences, Science & Technology - Other Topics, GENOME-WIDE ASSOCIATION, ADAPTER PROTEINS, MAMMALIAN-CELLS, CROHNS-DISEASE, IMMUNITY, UBIQUITIN, SUSCEPTIBILITY, SALMONELLA, INFLAMMATION, RECOGNITION, Autophagy, Cell Proliferation, Cytoplasm, Cytoplasmic Vesicles, Endosomes, Galectins, HeLa Cells, Humans, Lysosomes, Nuclear Proteins, Salmonella Infections, Salmonella typhimurium, MD Multidisciplinary, General Science & Technology

الوصف: Autophagy defends the mammalian cytosol against bacterial infection1,2,3. Efficient pathogen engulfment is mediated by cargo-selecting autophagy adaptors that rely on unidentified pattern-recognition or danger receptors to label invading pathogens as autophagy cargo, typically by polyubiquitin coating4,5,6,7,8,9. Here we show in human cells that galectin 8 (also known as LGALS8), a cytosolic lectin, is a danger receptor that restricts Salmonella proliferation. Galectin 8 monitors endosomal and lysosomal integrity and detects bacterial invasion by binding host glycans exposed on damaged Salmonella-containing vacuoles. By recruiting NDP52 (also known as CALCOCO2), galectin 8 activates antibacterial autophagy. Galectin-8-dependent recruitment of NDP52 to Salmonella-containing vesicles is transient and followed by ubiquitin-dependent NDP52 recruitment. Because galectin 8 also detects sterile damage to endosomes or lysosomes, as well as invasion by Listeria or Shigella, we suggest that galectin 8 serves as a versatile receptor for vesicle-damaging pathogens. Our results illustrate how cells deploy the danger receptor galectin 8 to combat infection by monitoring endosomal and lysosomal integrity on the basis of the specific lack of complex carbohydrates in the cytosol.

العلاقة: Nature; http://hdl.handle.net/10044/1/59053Test; https://dx.doi.org/10.1038/nature10744Test

الإتاحة: https://doi.org/10.1038/nature10744Test
http://hdl.handle.net/10044/1/59053Test