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Article: Resistance of Sugarcane Cultivar R 570 to Puccinia melanocephala Isolatesfrom Different Geographic Locations.

Asnaghi, C / D'Hont, A / Glaszmann, J C / Rott, P

2019 Volume 85, Issue 3, Page(s) 282–286

Abstract: ... rust resistance gene of sugarcane cultivar R 570 against isolates of Puccinia melanocephala ... from different geographic locations. Cultivar R 570 exhibited severe rust symptoms when in vitro plantlets were ... when detached leaves were inoculated with the pathogen. This latter technique was then used to inoculate R 570 ...

Abstract	Two different inoculation techniques were investigated before studying the reaction of the major rust resistance gene of sugarcane cultivar R 570 against isolates of Puccinia melanocephala from different geographic locations. Cultivar R 570 exhibited severe rust symptoms when in vitro plantlets were inoculated with a rust isolate from Réunion Island, but a good correlation with field resistance was observed when detached leaves were inoculated with the pathogen. This latter technique was then used to inoculate R 570 and a sample of its self progeny with rust isolates from Brazil, Colombia, Florida (three isolates), Guadeloupe, Réunion Island, and Zimbabwe. R 570 was resistant to all isolates of P. melanocephala, and the segregation of resistance in the progeny did not change with the isolates, suggesting that a single gene, or a single chromosomic region, was involved in the resistance against all tested isolates. This major resistance gene has, therefore, potential value to improve resistance to rust in various geographic regions.
Language	English
Publishing date	2019-03-04
Publishing country	United States
Document type	Journal Article
ZDB-ID	754182-x
ISSN	0191-2917
ISSN	0191-2917
DOI	10.1094/PDIS.2001.85.3.282
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Article ; Online: Genome sequence of Xanthomonas fuscans subsp. fuscans strain 4834-R reveals that flagellar motility is not a general feature of xanthomonads.

Darrasse, Armelle / Carrère, Sébastien / Barbe, Valérie / Boureau, Tristan / Arrieta-Ortiz, Mario L / Bonneau, Sophie / Briand, Martial / Brin, Chrystelle / Cociancich, Stéphane / Durand, Karine / Fouteau, Stéphanie / Gagnevin, Lionel / Guérin, Fabien / Guy, Endrick / Indiana, Arnaud / Koebnik, Ralf / Lauber, Emmanuelle / Munoz, Alejandra / Noël, Laurent D /

Pieretti, Isabelle / Poussier, Stéphane / Pruvost, Olivier / Robène-Soustrade, Isabelle / Rott, Philippe / Royer, Monique / Serres-Giardi, Laurana / Szurek, Boris / van Sluys, Marie-Anne / Verdier, Valérie / Vernière, Christian / Arlat, Matthieu / Manceau, Charles / Jacques, Marie-Agnès

BMC genomics

2013 Volume 14, Page(s) 761

Abstract: ... blight of bean. In this study, the complete genome sequence of strain Xff 4834-R was determined and ... characteristics shared between Xff 4834-R and other xanthomonads including chemotaxis elements, two-component ... 4834-R. The presence of a complete flagellar cluster was assessed in a collection of more than 300 ...

Abstract	Background: Xanthomonads are plant-associated bacteria responsible for diseases on economically important crops. Xanthomonas fuscans subsp. fuscans (Xff) is one of the causal agents of common bacterial blight of bean. In this study, the complete genome sequence of strain Xff 4834-R was determined and compared to other Xanthomonas genome sequences. Results: Comparative genomics analyses revealed core characteristics shared between Xff 4834-R and other xanthomonads including chemotaxis elements, two-component systems, TonB-dependent transporters, secretion systems (from T1SS to T6SS) and multiple effectors. For instance a repertoire of 29 Type 3 Effectors (T3Es) with two Transcription Activator-Like Effectors was predicted. Mobile elements were associated with major modifications in the genome structure and gene content in comparison to other Xanthomonas genomes. Notably, a deletion of 33 kbp affects flagellum biosynthesis in Xff 4834-R. The presence of a complete flagellar cluster was assessed in a collection of more than 300 strains representing different species and pathovars of Xanthomonas. Five percent of the tested strains presented a deletion in the flagellar cluster and were non-motile. Moreover, half of the Xff strains isolated from the same epidemic than 4834-R was non-motile and this ratio was conserved in the strains colonizing the next bean seed generations. Conclusions: This work describes the first genome of a Xanthomonas strain pathogenic on bean and reports the existence of non-motile xanthomonads belonging to different species and pathovars. Isolation of such Xff variants from a natural epidemic may suggest that flagellar motility is not a key function for in planta fitness.
MeSH term(s)	Base Sequence ; Evolution, Molecular ; Fabaceae/genetics ; Fabaceae/growth & development ; Fabaceae/microbiology ; Flagella/genetics ; Flagella/physiology ; Genetic Fitness ; Genome, Bacterial ; Phylogeny ; Plant Diseases/genetics ; Plant Diseases/microbiology ; Seeds/genetics ; Seeds/microbiology ; Sequence Analysis, DNA ; Xanthomonas/classification ; Xanthomonas/genetics ; Xanthomonas/pathogenicity
Language	English
Publishing date	2013-11-06
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2041499-7
ISSN	1471-2164 ; 1471-2164
ISSN (online)	1471-2164
ISSN	1471-2164
DOI	10.1186/1471-2164-14-761
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Article: Hemagglutinin activation of pathogenic avian influenza viruses of serotype H7 requires the protease recognition motif R-X-K/R-R.

Vey, M / Orlich, M / Adler, S / Klenk, H D / Rott, R / Garten, W

Virology

1992 Volume 188, Issue 1, Page(s) 408–413

Abstract: ... R-X-K/R-R that must be presented in the correct sequence position. Studies on plaque variants ...

Abstract	The hemagglutinin of influenza virus A/FPV/Rostock/34 (H7) was altered at its multibasic cleavage site by site-directed mutagenesis and assayed for proteolytic activation after expression in CV-1 cells. The results indicated that the cellular protease responsible for activation recognizes the tetrapeptide motif R-X-K/R-R that must be presented in the correct sequence position. Studies on plaque variants of influenza virus A/fowl/Victoria/75 (H7N7) showed that alteration of the consensus sequence resulted in a loss of pathogenicity for chickens.
MeSH term(s)	Amino Acid Sequence ; Base Sequence ; DNA, Viral ; Endopeptidases/metabolism ; Hemagglutinins, Viral/metabolism ; Influenza A virus/genetics ; Influenza A virus/metabolism ; Influenza A virus/pathogenicity ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Proline/metabolism
Chemical Substances	DNA, Viral ; Hemagglutinins, Viral ; Proline (9DLQ4CIU6V) ; Endopeptidases (EC 3.4.-)
Keywords	covid19
Language	English
Publishing date	1992-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	200425-2
ISSN	1096-0341 ; 0042-6822
ISSN (online)	1096-0341
ISSN	0042-6822
DOI	10.1016/0042-6822(92)90775-k
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Article: Darstellung und Charakterisierung von Spezies der Zusammensetzung η5-C5H5Cr(NO)2SR (R = C6H5, C6F5, t–C4H9) und [η5-C5H5CrNO]2(ER)2 (E = O, S, Se, Te, R = Alkyl, Aryl); Röntgenstrukturanalysen von [η5-C5H5(NO)Cr(μ-SeC6H5)2Cr(NO)-η5-C5H5] und [η5-C5H5(NO)Cr(μ-Se-n-C4H9)(μ-OH)Cr(NO)-η5-C5H5] / Synthesis and Characterization of Species of Composition η5-C5H5Cr(NO)2SR (R = C6H5, C6F5, t-C4H9) and [η5-C5H5CrNO]2(ER)2 (E = O, S, Se, Te, R = Alkyl, Aryl); Röntgenstrukturanalysen von [η5-C5H5(NO)Cr(μ-SeC6H5)2Cr(NO)-η5-C5H5] and [η5-C5H5(NO)Cr(μ-Se-n-C4H9)(μ-OH)Cr(NO)-η5-C5H5]

Rott, Johannes / Ernst Guggolz / Albert Rettenmeier / Manfred L. Ziegler

Zeitschrift für Naturforschung. 2014 June 2, v. 37, no. 1

2014

Abstract: The title compounds have been synthesized and characterized by elemental analysis, IR and ¹H NMR methods and mass spectra. The crystal and molecular structures of the binuclear complexes [η-C₅H₅(NO)Cr(μ-SeC₆H₅)₂Cr(NO)-η⁵-C₅H₅] and [η⁵-C₅H₅(NO)Crμ-Se-n-C₄ ... ...

Abstract	The title compounds have been synthesized and characterized by elemental analysis, IR and ¹H NMR methods and mass spectra. The crystal and molecular structures of the binuclear complexes [η-C₅H₅(NO)Cr(μ-SeC₆H₅)₂Cr(NO)-η⁵-C₅H₅] and [η⁵-C₅H₅(NO)Crμ-Se-n-C₄H₉)(μ-OH)Cr(NO)-μ⁵-C₅H₅] have been determined by X-ray structure analysis. The latter is shown to have a four-membered ring consisting of two chromium atoms, one selenium, and one oxygen atom.
Keywords	X-radiation ; chromium ; nitric oxide ; nuclear magnetic resonance spectroscopy ; oxygen ; selenium ; sulfur
Language	English
Dates of publication	2014-0602
Size	p. 13-23.
Publishing place	Verlag der Zeitschrift für Naturforschung
Document type	Article
ZDB-ID	124635-5
ISSN	0340-5087 ; 0044-3174 ; 0932-0776 ; 0341-0447 ; 0341-0420
ISSN	0340-5087 ; 0044-3174 ; 0932-0776 ; 0341-0447 ; 0341-0420
DOI	10.1515/znb-1982-0104
Database	NAL-Catalogue (AGRICOLA)

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Article: Indikationen und Ergebnisse der Anwendung von Desmopressin (DDAVP/Minirin(r))

Rott, H.

Journal für Anästhesie und Intensivbehandlung

2002 Volume -, Issue 4, Page(s) 40

Language	German
Document type	Article
ZDB-ID	1232203-9
Database	Current Contents Medicine

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Article: Determinants of pantropism of the F1-R mutant of Sendai virus: specific mutations involved are in the F and M genes.

Okada, H / Seto, J T / McQueen, N L / Klenk, H D / Rott, R / Tashiro, M

Archives of virology

1998 Volume 143, Issue 12, Page(s) 2343–2352

Abstract: ... F1-R. Several mutants of Sendai virus (BY, BF, and KD-M) with phenotypes of bipolar budding and/or ... R, T-5 (a revertant of F1-R), and wild-type viruses. The BF and KD-M mutants that budded bipolarly ... without trypsin, but formed plaques only in MDCK cells. One of the mutants, designated KD-52M, was similar to F1-R ...

Abstract	Mutations in the fusion, F, protein of Sendai virus resulting in increased cleavability by ubiquitous host protease(s), and mutations in the matrix, M, protein resulting in bipolar budding, are both important determinants for the systemic infection in mice caused by the protease activating pantropic mutant, F1-R. Several mutants of Sendai virus (BY, BF, and KD-M) with phenotypes of bipolar budding and/or increased cleavability of F protein were isolated. Genomic RNA sequence analysis of the F and M genes of the mutants revealed that several deduced amino acids in the F and M proteins were different from those of F1-R, T-5 (a revertant of F1-R), and wild-type viruses. The BF and KD-M mutants that budded bipolarly and were also activated by ubiquitous proteases were examined for replication in tissue culture cells and in mice. All of the mutants exhibited multiple-step replication in MDCK, MDBK, and LLC-MK2 cells without trypsin, but formed plaques only in MDCK cells. One of the mutants, designated KD-52M, was similar to F1-R in that it formed plaques in all three cell lines without addition of exogenous protease. However, none of the mutants viruses, including KD-52M, caused a systemic infection in mice. The mutated M protein of F1-R enhances the disruption of microtubles. However, none of the mutants with a bipolar budding phenotype (BY, BF, and KD-M), disrupted the microtubules to the same extent as F1-R. All of these mutants had mutations in the M protein that were different from those found in F1-R. Taken together, these results suggest that mutations at Ser115 to Pro in the F protein and at Asp 128 to Gly and Ile210 to Thr in the M protein of F1-R are the mutations specifically required for the systemic infection caused by F1-R.
MeSH term(s)	Amino Acid Sequence ; Animals ; Cattle ; Cell Line ; Cell Polarity ; Dogs ; Genes, Viral ; Genotype ; Mice ; Microtubules/physiology ; Molecular Sequence Data ; Mutation ; Phenotype ; Respirovirus/genetics ; Respirovirus/pathogenicity ; Respirovirus/physiology ; Respirovirus Infections/etiology ; Respirovirus Infections/virology ; Transfection ; Viral Fusion Proteins/genetics ; Viral Matrix Proteins/genetics ; Virulence/genetics ; Virus Replication/genetics
Chemical Substances	Viral Fusion Proteins ; Viral Matrix Proteins
Language	English
Publishing date	1998
Publishing country	Austria
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	7491-3
ISSN	1432-8798 ; 0304-8608
ISSN (online)	1432-8798
ISSN	0304-8608
DOI	10.1007/s007050050465
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Article: Search for pair production of scalar top quarks in R-parity violating decay modes in pp collisions at square root of s=1.8 TeV.

Acosta, D / Affolder, T / Akimoto, H / Albrow, M G / Ambrose, D / Amidei, D / Anikeev, K / Antos, J / Apollinari, G / Arisawa, T / Artikov, A / Asakawa, T / Ashmanskas, W / Azfar, F / Azzi-Bacchetta, P / Bacchetta, N / Bachacou, H / Badgett, W / Bailey, S /

de Barbaro, P / Barbaro-Galtieri, A / Barnes, V E / Barnett, B A / Baroiant, S / Barone, M / Bauer, G / Bedeschi, F / Behari, S / Belforte, S / Bell, W H / Bellettini, G / Bellinger, J / Benjamin, D / Bensinger, J / Beretvas, A / Berryhill, J / Bhatti, A / Binkley, M / Bisello, D / Bishai, M / Blair, R E / Blocker, C / Bloom, K / Blumenfeld, B / Blusk, S R / Bocci, A / Bodek, A / Bolla, G / Bolshov, A / Bonushkin, Y / Bortoletto, D / Boudreau, J / Brandl, A / Bromberg, C / Brozovic, M / Brubaker, E / Bruner, N / Budagov, J / Budd, H S / Burkett, K / Busetto, G / Byrum, K L / Cabrera, S / Calafiura, P / Campbell, M / Carithers, W / Carlson, J / Carlsmith, D / Caskey, W / Castro, A / Cauz, D / Cerri, A / Cerrito, L / Chan, A W / Chang, P S / Chang, P T / Chapman, J / Chen, C / Chen, Y C / Cheng, M-T / Chertok, M / Chiarelli, G / Chirikov-Zorin, I / Chlachidze, G / Chlebana, F / Christofek, L / Chu, M L / Chung, J Y / Chung, W-H / Chung, Y S / Ciobanu, C I / Clark, A G / Coca, M / Colijn, A P / Connolly, A / Convery, M / Conway, J / Cordelli, M / Cranshaw, J / Culbertson, R / Dagenhart, D / D'Auria, S / De Cecco, S / DeJongh, F / Dell'Agnello, S / Dell'Orso, M / Demers, S / Demortier, L / Deninno, M / De Pedis, D / Derwent, P F / Devlin, T / Dionisi, C / Dittmann, J R / Dominguez, A / Donati, S / D'Onofrio, M / Dorigo, T / Eddy, N / Einsweiler, K / Engels, E / Erbacher, R / Errede, D / Errede, S / Eusebi, R / Fan, Q / Farrington, S / Feild, R G / Fernandez, J P / Ferretti, C / Field, R D / Fiori, I / Flaugher, B / Flores-Castillo, L R / Foster, G W / Franklin, M / Freeman, J / Friedman, J / Fukui, Y / Furic, I / Galeotti, S / Gallas, A / Gallinaro, M / Gao, T / Garcia-Sciveres, M / Garfinkel, A F / Gatti, P / Gay, C / Gerdes, D W / Gerstein, E / Giagu, S / Giannetti, P / Giolo, K / Giordani, M / Giromini, P / Glagolev, V / Glenzinski, D / Gold, M / Goldschmidt, N / Goldstein, J / Gomez, G / Goncharov, M / Gorelov, I / Goshaw, A T / Gotra, Y / Goulianos, K / Green, C / Gresele, A / Grim, G / Grosso-Pilcher, C / Guenther, M / Guillian, G / Guimaraes da Costa, J / Haas, R M / Haber, C / Hahn, S R / Halkiadakis, E / Hall, C / Handa, T / Handler, R / Happacher, F / Hara, K / Hardman, A D / Harris, R M / Hartmann, F / Hatakeyama, K / Hauser, J / Heinrich, J / Heiss, A / Hennecke, M / Herndon, M / Hill, C / Hocker, A / Hoffman, K D / Hollebeek, R / Holloway, L / Hou, S / Huffman, B T / Hughes, R / Huston, J / Huth, J / Ikeda, H / Issever, C / Incandela, J / Introzzi, G / Iori, M / Ivanov, A / Iwai, J / Iwata, Y / Iyutin, B / James, E / Jones, M / Joshi, U / Kambara, H / Kamon, T / Kaneko, T / Kang, J / Karagoz Unel, M / Karr, K / Kartal, S / Kasha, H / Kato, Y / Keaffaber, T A / Kelley, K / Kelly, M / Kennedy, R D / Kephart, R / Khazins, D / Kikuchi, T / Kilminster, B / Kim, B J / Kim, D H / Kim, H S / Kim, M J / Kim, S B / Kim, S H / Kim, T H / Kim, Y K / Kirby, M / Kirk, M / Kirsch, L / Klimenko, S / Koehn, P / Kondo, K / Konigsberg, J / Korn, A / Korytov, A / Kotelnikov, K / Kovacs, E / Kroll, J / Kruse, M / Krutelyov, V / Kuhlmann, S E / Kurino, K / Kuwabara, T / Kuznetsova, N / Laasanen, A T / Lai, N / Lami, S / Lammel, S / Lancaster, J / Lannon, K / Lancaster, M / Lander, R / Lath, A / Latino, G / LeCompte, T / Le, Y / Lee, J / Lee, S W / Leonardo, N / Leone, S / Lewis, J D / Li, K / Lin, C S / Lindgren, M / Liss, T M / Liu, J B / Liu, T / Liu, Y C / Litvintsev, D O / Lobban, O / Lockyer, N S / Loginov, A / Loken, J / Loreti, M / Lucchesi, D / Lukens, P / Lusin, S / Lyons, L / Lys, J / Madrak, R / Maeshima, K / Maksimovic, P / Malferrari, L / Mangano, M / Manca, G / Mariotti, M / Martignon, G / Martin, M / Martin, A / Martin, V / Martínez, M / Matthews, J A J / Mazzanti, P / McFarland, K S / McIntyre, P / Menguzzato, M / Menzione, A / Merkel, P / Mesropian, C / Meyer, A / Miao, T / Miller, R / Miller, J S / Minato, H / Miscetti, S / Mishina, M / Mitselmakher, G / Miyazaki, Y / Moggi, N / Moore, E / Moore, R / Morita, Y / Moulik, T / Mulhearn, M / Mukherjee, A / Muller, T / Munar, A / Murat, P / Murgia, S / Nachtman, J / Nagaslaev, V / Nahn, S / Nakada, H / Nakano, I / Napora, R / Niell, F / Nelson, C / Nelson, T / Neu, C / Neubauer, M S / Neuberger, D / Newman-Holmes, C / Ngan, C-Y P / Nigmanov, T / Niu, H / Nodulman, L / Nomerotski, A / Oh, S H / Oh, Y D / Ohmoto, T / Ohsugi, T / Oishi, R / Okusawa, T / Olsen, J / Orejudos, W / Pagliarone, C / Palmonari, F / Paoletti, R / Papadimitriou, V / Partos, D / Patrick, J / Pauletta, G / Paulini, M / Pauly, T / Paus, C / Pellett, D / Penzo, A / Pescara, L / Phillips, T J / Piacentino, G / Piedra, J / Pitts, K T / Pompos, A / Pondrom, L / Pope, G / Pratt, T / Prokoshin, F / Proudfoot, J / Ptohos, F / Pukhov, O / Punzi, G / Rademacker, J / Rakitine, A / Ratnikov, F / Ray, H / Reher, D / Reichold, A / Renton, P / Rescigno, M / Ribon, A / Riegler, W / Rimondi, F / Ristori, L / Riveline, M / Robertson, W J / Rodrigo, T / Rolli, S / Rosenson, L / Roser, R / Rossin, R / Rott, C / Roy, A / Ruiz, A / Ryan, D / Safonov, A / St Denis, R / Sakumoto, W K / Saltzberg, D / Sanchez, C / Sansoni, A / Santi, L / Sarkar, S / Sato, H / Savard, P / Savoy-Navarro, A / Schlabach, P / Schmidt, E E / Schmidt, M P / Schmitt, M / Scodellaro, L / Scott, A / Scribano, A / Sedov, A / Seidel, S / Seiya, Y / Semenov, A / Semeria, F / Shah, T / Shapiro, M D / Shepard, P F / Shibayama, T / Shimojima, M / Shochet, M / Sidoti, A / Siegrist, J / Sill, A / Sinervo, P / Singh, P / Slaughter, A J / Sliwa, K / Snider, F D / Snihur, R / Solodsky, A / Spalding, J / Speer, T / Spezziga, M / Sphicas, P / Spinella, F / Spiropulu, M / Spiegel, L / Steele, J / Stefanini, A / Strologas, J / Strumia, F / Stuart, D / Sukhanov, A / Sumorok, K / Suzuki, T / Takano, T / Takashima, R / Takikawa, K / Tamburello, P / Tanaka, M / Tannenbaum, B / Tecchio, M / Tesarek, R J / Teng, P K / Terashi, K / Tether, S / Thom, J / Thompson, A S / Thomson, E / Thurman-Keup, R / Tipton, P / Tkaczyk, S / Toback, D / Tollefson, K / Tonelli, D / Tonnesmann, M / Toyoda, H / Trischuk, W / De Troconiz, J F / Tseng, J / Tsybychev, D / Turini, N / Ukegawa, F / Unverhau, T / Vaiciulis, T / Valls, J / Varganov, A / Vataga, E / Vejcik, S / Velev, G / Veramendi, G / Vidal, R / Vila, I / Vilar, R / Volobouev, I / von der Mey, M / Vucinic, D / Wagner, R G / Wagner, R L / Wagner, W / Wallace, N B / Wan, Z / Wang, C / Wang, M J / Wang, S M / Ward, B / Waschke, S / Watanabe, T / Waters, D / Watts, T / Weber, M / Wenzel, H / Wester, W C / Whitehouse, B / Wicklund, A B / Wicklund, E / Wilkes, T / Williams, H H / Wilson, P / Winer, B L / Winn, D / Wolbers, S / Wolinski, D / Wolinski, J / Wolinski, S / Wolter, M / Worm, S / Wu, X / Würthwein, F / Wyss, J / Yang, U K / Yao, W / Yeh, G P / Yeh, P / Yi, K / Yoh, J / Yosef, C / Yoshida, T / Yu, I / Yu, S / Yu, Z / Yun, J C / Zanello, L / Zanetti, A / Zetti, F / Zucchelli, S

Physical review letters

2004 Volume 92, Issue 5, Page(s) 51803

Abstract: We present the results of a search for pair production of scalar top quarks (t(1)) in an R-parity ...

Abstract	We present the results of a search for pair production of scalar top quarks (t(1)) in an R-parity violating supersymmetry scenario in 106 pb(-1) of pp collisions at square root of s=1.8 TeV collected by the Collider Detector at Fermilab. In this mode each t(1) decays into a tau lepton and a b quark. We search for events with two tau's, one decaying leptonically (e or mu) and one decaying hadronically, and two jets. No candidate events pass our final selection criteria. We set a 95% confidence level lower limit on the t(1) mass at 122 GeV/c(2) for Br(t(1)-->tau b)=1.
Language	English
Publishing date	2004-02-06
Publishing country	United States
Document type	Journal Article
ZDB-ID	208853-8
ISSN	1079-7114 ; 0031-9007
ISSN (online)	1079-7114
ISSN	0031-9007
DOI	10.1103/PhysRevLett.92.051803
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Article: Pneumotropic revertants derived from a pantropic mutant, F1-R, of Sendai virus.

Tashiro, M / James, I / Karri, S / Wahn, K / Tobita, K / Klenk, H D / Rott, R / Seto, J T

Virology

1991 Volume 184, Issue 1, Page(s) 227–234

Abstract: Revertants were isolated from the protease activation mutant of Sendai virus, F1-R, which causes ... a systemic infection in mice. The fusion (F) glycoprotein of F1-R is susceptible to activation cleavage ... exclusively pneumotropic in mice. On the other hand, phenotypes of F1-R that remained unchanged ...

Abstract	Revertants were isolated from the protease activation mutant of Sendai virus, F1-R, which causes a systemic infection in mice. The fusion (F) glycoprotein of F1-R is susceptible to activation cleavage by ubiquitous cellular proteases and is thus responsible for pantropism in mice (Tashiro et al., 1988. Virology 165, 577-583). The revertants regained several phenotypes of wild-type virus; they required exogenous trypsin for activation of the F protein in cell cultures and in nonpulmonary mouse tissues and they were exclusively pneumotropic in mice. On the other hand, phenotypes of F1-R that remained unchanged by the revertants were bipolar budding in polarized epithelial cells, enhanced electrophoretic migration of the matrix protein, and the lack of a glycosylation site in the F2 subunit of the F protein. Comparative RNA sequence analysis of the F gene of the revertants revealed that the reduced cleavability of the F protein of the revertants was the result of the predicted single amino acid reversion (Pro to Ser) at residue 115 adjacent to the cleavage site. Thus the sequence at the cleavage site of the revertants was Ser-Lys compared with Pro-Lys for F1-R and Ser-Arg for wild-type virus. The results indicate that enhanced cleavability of the glycoprotein, a feature often associated with multiple basic residues within the cleavage site of paramyxovirus F proteins and influenza virus hemagglutinins, can also be determined by a single basic amino acid following proline. Additionally, the revertants were less susceptible to the activator for wild-type virus present in mouse lungs and less pathogenic for this organ than wild-type virus. These results provide further evidence that proteolytic activation of the F protein by host proteases is the primary determinant for organ tropism and pathogenicity of Sendai virus in mice. One of the revertants was also temperature sensitive (ts); the ts lesion in the nucleoprotein gene was identical to that found in ts-f1, the ts host range mutant from which F1-R was derived.
MeSH term(s)	Amino Acid Sequence ; Animals ; Endopeptidases/metabolism ; Male ; Mice ; Mice, Inbred ICR ; Molecular Sequence Data ; Organ Culture Techniques ; Parainfluenza Virus 1, Human/genetics ; Parainfluenza Virus 1, Human/growth & development ; Parainfluenza Virus 1, Human/pathogenicity ; Paramyxoviridae Infections/pathology ; Paramyxoviridae Infections/physiopathology ; Viral Fusion Proteins/genetics ; Viral Fusion Proteins/metabolism ; Viral Plaque Assay ; Viral Proteins/genetics ; Virus Activation
Chemical Substances	Viral Fusion Proteins ; Viral Proteins ; Endopeptidases (EC 3.4.-)
Language	English
Publishing date	1991-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	200425-2
ISSN	1096-0341 ; 0042-6822
ISSN (online)	1096-0341
ISSN	0042-6822
DOI	10.1016/0042-6822(91)90839-4
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Article: Hemagglutinin activation of pathogenic avian influenza viruses of serotype H7 requires the protease recognition motif R-X-K/R-R

Vewy, M / Orlich, M / Adler, S / Klenk, H.D / Rott, R / Garten, W

Virology. May 1992. v. 188 (1)

1992

Abstract: ... R-X-K/R-R that must be presented in the correct sequence position. Studies on plaque variants ...

Abstract	The hemagglutinin of influenza virus A/FPV/Rostock/34 (H7) was altered at its multibasic cleavage site by site-directed mutagenesis and assayed for proteolytic activation after expression in CV-1 cells. The results indicated that the cellular protease responsible for activation recognizes the tetrapeptide motif R-X-K/R-R that must be presented in the correct sequence position. Studies on plaque variants of influenza virus A/fowl/Victoria/75 (H7N7) showed that alteration of the consensus sequence resulted in a loss of pathogenicity for chickens.
Keywords	chickens ; Influenza A virus ; proteinases ; proteolysis ; amino acid sequences ; mutants ; clones ; pathogenicity
Language	English
Dates of publication	1992-05
Size	p. 408-413.
Document type	Article
ZDB-ID	200425-2
ISSN	1096-0341 ; 0042-6822
ISSN (online)	1096-0341
ISSN	0042-6822
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Article: Involvement of the mutated M protein in altered budding polarity of a pantropic mutant, F1-R, of Sendai virus.

Tashiro, M / McQueen, N L / Seto, J T / Klenk, H D / Rott, R

Journal of virology

1996 Volume 70, Issue 9, Page(s) 5990–5997

Abstract: ... proteins in F1-R are responsible for these changes (M. Tashiro, J. T. Seto, H.-D. Klenk, and R. Rott, J ... whereas a pantropic mutant, F1-R, buds at both the apical and basolateral domains. In F1-R-infected cells, polarized ... disruption which leads to altered budding of F1-R, MDCK cell lines containing the M gene of either the wild ...

Abstract	Wild-type Sendai virus buds at the apical plasma membrane domain of polarized epithelial MDCK cells, whereas a pantropic mutant, F1-R, buds at both the apical and basolateral domains. In F1-R-infected cells, polarized protein transport and the microtubule network are impaired. It has been suggested that the mutated F and/or M proteins in F1-R are responsible for these changes (M. Tashiro, J. T. Seto, H.-D. Klenk, and R. Rott, J. Virol. 67:5902-5910, 1993). To clarify which gene or mutation(s) was responsible for the microtubule disruption which leads to altered budding of F1-R, MDCK cell lines containing the M gene of either the wild type or F1-R were established. When wild-type M protein was expressed at a level corresponding to that synthesized in virus-infected cells, cellular polarity and the integrity of the microtubules were affected to some extent. On the other hand, expression of the mutated F1-R M protein resulted in the formation of giant cells about 40 times larger than normal MDCK cells. Under these conditions, the effects on the microtubule network were enhanced. The microtubules were disrupted and polarized protein transport was impaired as indicated by the nonpolarized secretion of gp80, a host cell glycoprotein normally secreted from the apical domain, and bipolar budding of wild-type and F1-R Sendai viruses. The mutated F glycoprotein of F1-R was transported bipolarly in cells expressing the F1-R M protein, whereas it was transported predominantly to the apical domain when expressed alone or in cells coexpressing the wild-type M protein. These findings indicate that the M protein of F1-R is involved in the disruption of the microtubular network, leading to impairment of cellular polarity, bipolar transport of the F glycoprotein, and bipolar budding of the virus.
MeSH term(s)	Animals ; Antibodies ; Antibodies, Monoclonal ; Cell Division/drug effects ; Cell Line ; Cell Membrane/virology ; Chick Embryo ; Dogs ; Epithelium ; Mice ; Microtubules/physiology ; Microtubules/ultrastructure ; Mutation ; Nocodazole/pharmacology ; Parainfluenza Virus 1, Human/genetics ; Parainfluenza Virus 1, Human/growth & development ; Parainfluenza Virus 1, Human/physiology ; Rabbits ; Viral Matrix Proteins/genetics ; Viral Matrix Proteins/metabolism ; Zinc/pharmacology
Chemical Substances	Antibodies ; Antibodies, Monoclonal ; M protein, Sendai virus ; Viral Matrix Proteins ; Zinc (J41CSQ7QDS) ; Nocodazole (SH1WY3R615)
Language	English
Publishing date	1996-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.70.9.5990-5997.1996
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