Microsporidian infection inPimpla turionellae (Ichneumonidae, Hymenoptera): characteristics and reaction with Calcofluor White

1989 ◽  
Vol 76 (1) ◽  
pp. 74-79 ◽  
Author(s):  
I. Pavenst�dt-Grupp ◽  
A. Ruthmann
2021 ◽  
Vol 184 ◽  
pp. 106202
Author(s):  
Biao Chen ◽  
Wenqiang Li ◽  
Yin Pang ◽  
Ning Zhang ◽  
Shaodong Bian ◽  
...  

Genetics ◽  
2003 ◽  
Vol 165 (2) ◽  
pp. 517-529
Author(s):  
Kentaro Ohkuni ◽  
Asuko Okuda ◽  
Akihiko Kikuchi

AbstractNbp2p is a Nap1-binding protein in Saccharomyces cerevisiae identified by its interaction with Nap1 by a two-hybrid system. NBP2 encodes a novel protein consisting of 236 amino acids with a Src homology 3 (SH3) domain. We showed that NBP2 functions to promote mitotic cell growth at high temperatures and cell wall integrity. Loss of Nbp2 results in cell death at high temperatures and in sensitivity to calcofluor white. Cell death at high temperature is thought not to be due to a weakened cell wall. Additionally, we have isolated several type-2C serine threonine protein phosphatases (PTCs) as multicopy suppressors and MAP kinase-kinase (MAPKK), related to the yeast PKC MAPK pathway, as deletion suppressors of the nbp2Δ mutant. Screening for deletion suppressors is a new genetic approach to identify and characterize additional proteins in the Nbp2-dependent pathway. Genetic analyses suggested that Ptc1, which interacts with Nbp2 by the two-hybrid system, acts downstream of Nbp2 and that cells lacking the function of Nbp2 prefer to lose Mkk1, but the PKC MAPK pathway itself is indispensable when Nbp2 is deleted at high temperature.


1996 ◽  
Vol 12 (5) ◽  
pp. 333-335 ◽  
Author(s):  
PAUL J. HONIG ◽  
KRISTIN SULLIVAN ◽  
KARIN L. McGOWAN

1977 ◽  
Vol 55 (11) ◽  
pp. 1445-1452 ◽  
Author(s):  
D. J. Samborski ◽  
W. K. Kim ◽  
R. Rohringer ◽  
N. K. Howes ◽  
R. J. Baker

Seedlings of resistant (Sr6) and susceptible (sr6) near-isogenic lines of wheat (Triticum aestivum L.) were inoculated with a race of stem rust (Puccinia graminis Pers. f. sp. tritici Eriks. & E. Henn.) that was avirulent on the line with Sr6 and they were kept at 19, 25, 26, and 27 °C. Fluorescence microscopy was used to detect autofluorescing necrotic host cells and rust colonies after these were stained with a fiuorochrome (Calcofluor White M2R New).In leaves containing the Sr6 gene, a smaller percentage of colonies grown at 25 °C had necrotic cells associated with them than those that were grown at 19 °C. The incidence of colony-associated necrosis in these leaves could be further reduced by increasing the temperature to 26 °C and 27 °C. Similarly, the number of necrotic host cells per colony decreased with an increase in temperature. Colonies in genotypically resistant leaves were usually smaller than those in genotypically susceptible leaves, but the differences in colony sizes between these two lines decreased at the higher temperatures.When infected plants containing the Sr6 gene were kept for varying times at 25 °C and then were transferred to 19 °C, there was significantly less fungal growth and more necrosis than in plants kept continuously at 25 °C. This necrosis occurred largely in those cells that were invaded after the transfer to 19 °C, when the Sr6 gene was activated.


2006 ◽  
Vol 6 (2) ◽  
pp. 328-336 ◽  
Author(s):  
Kariona A. Grabińska ◽  
Paula Magnelli ◽  
Phillips W. Robbins

ABSTRACT Chs4p (Cal2/Csd4/Skt5) was identified as a protein factor physically interacting with Chs3p, the catalytic subunit of chitin synthase III (CSIII), and is indispensable for its enzymatic activity in vivo. Chs4p contains a putative farnesyl attachment site at the C-terminal end (CVIM motif) conserved in Chs4p of Saccharomyces cerevisiae and other fungi. Several previous reports questioned the role of Chs4p prenylation in chitin biosynthesis. In this study we reinvestigated the function of Chs4p prenylation. We provide evidence that Chs4p is farnesylated by showing that purified Chs4p is recognized by anti-farnesyl antibody and is a substrate for farnesyl transferase (FTase) in vitro and that inactivation of FTase increases the amount of unmodified Chs4p in yeast cells. We demonstrate that abolition of Chs4p prenylation causes a ∼60% decrease in CSIII activity, which is correlated with a ∼30% decrease in chitin content and with increased resistance to the chitin binding compound calcofluor white. Furthermore, we show that lack of Chs4p prenylation decreases the average chain length of the chitin polymer. Prenylation of Chs4p, however, is not a factor that mediates plasma membrane association of the protein. Our results provide evidence that the prenyl moiety attached to Chs4p is a factor modulating the activity of CSIII both in vivo and in vitro.


Cellulose ◽  
2018 ◽  
Vol 26 (2) ◽  
pp. 971-977
Author(s):  
Roi Peretz ◽  
Hadas Mamane ◽  
Elizaveta Sterenzon ◽  
Yoram Gerchman

2003 ◽  
Vol 78 (5) ◽  
pp. 547-551 ◽  
Author(s):  
Keith Werneck Brasil ◽  
Rosângela Lameira Pinheiro ◽  
Ida Chapaval Pimentel
Keyword(s):  

FUNDAMENTOS: As micoses superficiais e cutâneas têm surgido com grande prevalência no Hospital de Clínicas da Universidade Federal do Paraná. OBJETIVOS: Avaliar o método do calcofluor white (CFW) mediante comparação com o método do hidróxido de potássio (KOH). MÉTODOS: Foram analisadas 74 amostras de raspados de pele, unha, couro cabeludo e cabelo de 62 pacientes de ambos os sexos em diferentes idades. O material foi coletado nos Ambulatórios de Dermatologia, Dermatopediatria e Pronto Atendimento do Hospital de Clínicas da Universidade Federal do Paraná, entre outubro de 1995 e março de 1996. Os espécimes foram analisados por ambos os métodos e comparados no presente trabalho. Os resultados obtidos foram submetidos à análise estatística do Qui-quadrado. RESULTADOS: Os resultados obtidos indicaram o CFW tão efetivo quanto o KOH. O hidróxido de potássio apresentou 38 (51%) resultados positivos e 36 (49%) negativos. O calcofluor white foi positivo em 35 (47%) amostras e negativo em 39 (53%). CONCLUSÃO: Os dados revelaram igual eficácia entre os métodos avaliados; no entanto, o método do calcofluor white necessita de um laboratório equipado com microscópio de imunofluorescência.


1991 ◽  
Vol 13 (1) ◽  
pp. 3-5 ◽  
Author(s):  
Brian J. Harrington ◽  
George J. Hageage
Keyword(s):  

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