Local Maladaptation in the Anther-Smut Fungus Microbotryum violaceum to Its Host Plant Silene latifolia: Evidence from a Cross-Inoculation Experiment

Evolution ◽  
1999 ◽  
Vol 53 (2) ◽  
pp. 395 ◽  
Author(s):  
Oliver Kaltz ◽  
Sylvain Gandon ◽  
Yannis Michalakis ◽  
Jacqui A. Shykoff
Keyword(s):  
Host Plant ◽  
Silene Latifolia ◽  
Smut Fungus ◽  
Inoculation Experiment ◽  
Microbotryum Violaceum ◽  
Anther Smut

scholarly journals Mating System of the Anther Smut Fungus Microbotryum violaceum: Selfing under Heterothallism

2008 ◽  
Vol 7 (5) ◽  
pp. 765-775 ◽  
Author(s):  
Tatiana Giraud ◽  
Roxana Yockteng ◽  
Manuela López-Villavicencio ◽  
Guislaine Refrégier ◽  
Michael E. Hood
Keyword(s):  
Mating System ◽  
Smut Fungus ◽  
Microbotryum Violaceum ◽  
Anther Smut

Morphological development of anthers induced by the dimorphic smut fungus Microbotryum violaceum in female flowers of the dioecious plant Silene latifolia

Planta ◽  
2003 ◽  
Vol 218 (2) ◽  
pp. 240-248 ◽  
Author(s):  
Wakana Uchida ◽  
Sachihiro Matsunaga ◽  
Ryuji Sugiyama ◽  
Yusuke Kazama ◽  
Shigeyuki Kawano
Keyword(s):  
Silene Latifolia ◽  
Smut Fungus ◽  
Morphological Development ◽  
Dioecious Plant ◽  
Microbotryum Violaceum ◽  
Female Flowers

Fimbrial-dependent mating inMicrobotryum violaceuminvolves a mannose–lectin interaction

1996 ◽  
Vol 42 (5) ◽  
pp. 461-466 ◽  
Author(s):  
Alan J. Castle ◽  
Nadia Stocco ◽  
Robert Boulianne
Keyword(s):  
Cell Adhesion ◽  
Concanavalin A ◽  
Smut Fungus ◽  
Mating Types ◽  
Carbohydrate Component ◽  
Microbotryum Violaceum ◽  
Anther Smut ◽  
Cell To Cell Adhesion ◽  
Fimbrial Protein ◽  
Dependent Mechanism

Fimbriae of the anther smut fungus, Microbotryum violaceum are polymers of six 74-kDa glycoprotein isoforms. Digestion of fimbrial monomers with α-mannosidase yielded two polypeptides with masses of 70 and 48 kDa. The 70-kDa polypeptide is probably a product of incomplete digestion and the 48-kDa polypeptide is the aglycone. Thus, most of the carbohydrate component of fimbrial protein is mannose. Previous observations have suggested that fimbriae are necessary for mating in M. violaceum. Further evidence for this role was obtained in the present study by showing that mating is inhibited by an anti-fimbrial protein antiserum, by mannose and related sugars glucose and arabinose, and by the lectin concanavalin A. Since inhibition was not complete, however, two mechanisms for adhesion between compatible cells were proposed, one fimbrial dependent and one independent. Lastly, fimbrial protein from a1but not a2mating types bound to a mannose–agarose column, suggesting a lectin-like capability. The fimbrial dependent mechanism of cell-to-cell adhesion may involve binding of the mannose residues of the fimbriae of a2cells by the fimbriae of a1cells.Key words: mating, Microbotryum violaceum, lectin, fimbriae.

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