scholarly journals The Whole Genome Sequence of a Novel Chrysovirus From Beauveria Bassiana Vuillemin, an Entomopathogenic Fungus

Author(s):  
Le Li ◽  
Qin Kang ◽  
Song-Bai Zhang ◽  
Du Hai ◽  
Yang Lu ◽  
...  

Abstract Beauveria bassiana, an entomopathogenic fungus, has a wide host range and is used for arthropod pest control worldwide. Here, we report the discovery and characterization of a novel double-stranded RNA (dsRNA) mycovirus Beauveria bassiana chrysovirus 2 (BbCV2), isolated from the B. bassiana from China. The genome of the virus was determined by metagenomic sequencing, RT-PCR, and RACE cloning comprises four dsRNA segments that are 3441bp, 2779bp, 2925bp, and 2688bp long, respectively, each of them contains a single ORF, the first one (ORF1) encoding a 1115-amino-acid-long protein (122.65 kDa) with a conserved RNA-dependent RNA polymerase (RdRp) motif, its sequences showed the highest identity of only 16.13% to that of the Beauveria bassiana chrysovirus 1. The second ORF (ORF-2) encoding a 807-amino-acid-long coat protein (CP) (88.77 kDa). The virus constitutes a new member of the chrysoviridea family from B. bassiana.

2016 ◽  
Vol 100 (20) ◽  
pp. 8889-8900 ◽  
Author(s):  
Sihyeon Kim ◽  
Se Jin Lee ◽  
Yu-Shin Nai ◽  
Jeong Seon Yu ◽  
Mi Rong Lee ◽  
...  

2010 ◽  
Vol 56 (11) ◽  
pp. 934-942 ◽  
Author(s):  
Sheng-Hua Ying ◽  
Xiao-Hui Wang ◽  
Ming-Guang Feng

A thioredoxin (BbTrx) was identified from the entomopathogenic fungus Beauveria bassiana . The cloned nucleotide sequence consisted of a 423-bp open reading frame encoding a 141-amino-acid thioredoxin, a 1011-bp 5′ region, and a 419-bp 3′ region. The deduced protein sequence of BbTrx, including a common 95-amino-acid conserved domain and a unique 46-amino-acid carboxy terminal region, was similar (≤38% identity) to that of other thioredoxins and phylogenetically closest to that from Neurospora crassa . In insulin solution containing dithiothreitol at 25 °C, recombinant BbTrx or a truncated form lacking the carboxy terminal region (BbTrxD) exhibited disulfide reduction activity. BbTrxD was more active after pre-incubation at 40–75 °C, and cells expressing BbTrxD showed significantly higher tolerance to thermal stress (51 °C). The BbTrx expression in B. bassiana was greatly elevated when stressed at 40 °C. The results indicate that the new thioredoxin is a potential target for improving the thermotolerance of B. bassiana formulations.


Parasitology ◽  
2007 ◽  
Vol 134 (14) ◽  
pp. 1989-1999 ◽  
Author(s):  
H. TACHIBANA ◽  
X.-J. CHENG ◽  
S. KOBAYASHI ◽  
Y. OKADA ◽  
J. ITOH ◽  
...  

SUMMARYWe have recently identified 2 surface proteins inEntamoeba histolyticaas intermediate subunits of galactose- andN-acetyl-D-galactosamine-inhibitable lectin (EhIgl1 and EhIgl2); these proteins both contain multiple CXXC motifs. Here, we report the molecular characterization of the corresponding proteins inEntamoeba dispar, which is neither pathogenic nor invasive. TwoIglgenes encoding 1110 and 1106 amino acids (EdIgl1 and EdIgl2) were cloned from 2 strains ofE. dispar. The amino acid sequence identities were 79% between EdIgl1 and EdIgl2, 75–76% between EdIgl1 and EhIgl1, and 73–74% between EdIgl2 and EhIgl2. However, all the CXXC motifs were conserved in the EdIgl proteins, suggesting that the fold conferred by this motif is important for function. Comparison of the expression level of theIglgenes by real-time RT-PCR showed 3–5 times higher expression ofEdIgl1compared toEdIgl2. Most EdIgl1 and EdIgl2 proteins were co-localized on the surface and in the cytoplasm of trophozoites, based on confocal microscopy. However, a different localization of EdIgl1 and EdIgl2 in intracellular vacuoles and a different level of phenotypic expression of the two Igls were also observed. These results demonstrate that Igls are important proteins even in non-pathogenic amoeba and that Igl1 and Igl2 may possess different functions.


2008 ◽  
Vol 55 (3) ◽  
pp. 473-478
Author(s):  
Nie Fa-Hui ◽  
Yao Hai-Feng ◽  
Qi Rui-Feng ◽  
Li Xin ◽  
Wu Cai-Bin

Human STAU1 is one member of the family of double-stranded RNA (dsRNA)-binding proteins. It is thought to function in transporting mRNA, controlling translation and eliciting mRNA decay in neurons, and to function in infection of influenza virus and human immunodeficiency virus type 1 (HIV-1). Four transcripts coding two isoforms have been identified before. In this study, we have isolated a novel transcript of STAU1, coding a novel isoform that has six amino acids more (SFPLKQ) than isoform a. In order to examine the tissue distribution of this novel isoform, we have performed RT-PCR experiments and the analysis showed that it was highly expressed in heart, liver, kidney and pancreas.


2021 ◽  
Author(s):  
Samira Mokhtari ◽  
Akhtar Ali

Abstract A double-stranded RNA (dsRNA) mycovirus was isolated from airborne spores of Fusarium bullatum and was named Fusarium bullatum alternavirus 1 (FbAV1). Sequencing analysis and the rapid amplification of cDNA ends (RACE) of 5’ and 3’-end confirmed three segments: dsRNA1 (3546 nt), dsRNA2 (2511 nt) and dsRNA3 (2484 nt). BLASTN search of sequences showed that FbAV1 has 92-96% identity with Fusarium incarnatum Alternavirus 1 (FiAV1). Phylogenetic analysis of the RdRp amino acid sequences suggested that the dsRNA mycovirus in this study clustered with the newly proposed family “Alternaviridae”. This is the first report of FbAV1 mycovirus from airborne spores of a fungus F. bullatum.


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