Considering amino acid sequence similarity of toxins for development of sustainable Bt crop pyramids

2016 ◽  
Author(s):  
Yves Carriere
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Similarity ◽  
Amino Acid Sequence Similarity ◽  
Bt Crop

scholarly journals Engineered Resistance Against Papaya ringspot virus in Venezuelan Transgenic Papayas

Plant Disease ◽  
2004 ◽  
Vol 88 (5) ◽  
pp. 516-522 ◽  
Author(s):  
Gustavo Fermin ◽  
Valentina Inglessis ◽  
Cesar Garboza ◽  
Sairo Rangel ◽  
Manuel Dagert ◽  
...  
Keyword(s):  
Amino Acid ◽  
Agrobacterium Tumefaciens ◽  
Coat Protein ◽  
Amino Acid Sequence ◽  
Sequence Similarity ◽  
Ringspot Virus ◽  
Amino Acid Sequence Similarity ◽  
Papaya Ringspot Virus ◽  
Local Varieties ◽  
Cp Gene

Local varieties of papaya grown in the Andean foothills of Mérida, Venezuela, were transformed independently with the coat protein (CP) gene from two different geographical Papaya ringspot virus (PRSV) isolates, designated VE and LA, via Agrobacterium tumefaciens. The CP genes of both PRSV isolates show 92 and 96% nucleotide and amino acid sequence similarity, respectively. Four PRSV-resistant R0 plants were intercrossed or selfed, and the progenies were tested for resistance against the homologous isolates VE and LA, and the heterologous isolates HA (Hawaii) and TH (Thailand) in greenhouse conditions. Resistance was affected by sequence similarity between the transgenes and the challenge viruses: resistance values were higher for plants challenged with the homologous isolates (92 to 100% similarity) than with the Hawaiian (94% similarity) and, lastly, Thailand isolates (88 to 89% similarity). Our results show that PRSV CP gene effectively protects local varieties of papaya against homologous and heterologous isolates of PRSV.

scholarly journals High-Efficiency Utilization of the Bovine Integrin αvβ3 as a Receptor for Foot-and-Mouth Disease Virus Is Dependent on the Bovine β3Subunit

2000 ◽  
Vol 74 (16) ◽  
pp. 7298-7306 ◽  
Author(s):  
Sherry Neff ◽  
Peter W. Mason ◽  
Barry Baxt
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Disease Virus ◽  
Sequence Similarity ◽  
Foot And Mouth Disease ◽  
Viral Proteins ◽  
Mouth Disease ◽  
Amino Acid Sequence Similarity ◽  
Mouth Disease Virus ◽  
Human Integrin

ABSTRACT We have previously reported that Foot-and-mouth disease virus (FMDV), which is virulent for cattle and swine, can utilize the integrin αvβ3 as a receptor on cultured cells. Since those studies were performed with the human integrin, we have molecularly cloned the bovine homolog of the integrin αvβ3 and have compared the two receptors for utilization by FMDV. Both the αv and β3subunits of the bovine integrin have high degrees of amino acid sequence similarity to their corresponding human subunits in the ectodomains (96%) and essentially identical transmembrane and cytoplasmic domains. Within the putative ligand-binding domains, the bovine and human αv subunits have a 98.8% amino acid sequence similarity while there is only a 93% similarity between the β3 subunits of these two species. COS cell cultures, which are not susceptible to FMDV infection, become susceptible if cotransfected with αv and β3 subunit cDNAs from a bovine or human source. Cultures cotransfected with the bovine αvβ3 subunit cDNAs and infected with FMDV synthesize greater amounts of viral proteins than do infected cultures cotransfected with the human integrin subunits. Cells cotransfected with a bovine αv subunit and a human β3subunit synthesize viral proteins at levels equivalent to those in cells expressing both human subunits. However, cells cotransfected with the human αv and the bovine β3 subunits synthesize amounts of viral proteins equivalent to those in cells expressing both bovine subunits, indicating that the bovine β3 subunit is responsible for the increased effectiveness of this receptor. By engineering chimeric bovine-human β3subunits, we have shown that this increase in receptor efficiency is due to sequences encoding the C-terminal one-third of the subunit ectodomain, which contains a highly structured cysteine-rich repeat region. We postulate that amino acid sequence differences within this region may be responsible for structural differences between the human and bovine β3 subunit, leading to more efficient utilization of the bovine receptor by this bovine pathogen.

scholarly journals The Moraxella bovis RTX toxin locus mbx defines a pathogenicity island

2006 ◽  
Vol 55 (4) ◽  
pp. 443-449 ◽  
Author(s):  
John F. Hess ◽  
John A. Angelos
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Mobile Genetic Element ◽  
Sequence Similarity ◽  
Pathogenicity Island ◽  
Amino Acid Sequence Similarity ◽  
Genetic Element ◽  
Genetic Organization ◽  
Moraxella Bovis ◽  
Flanking Regions

To characterize flanking regions of the mbx operon in Moraxella bovis, DNA surrounding mbxCABDtolC was sequenced in haemolytic and nonhaemolytic strains of M. bovis. In two haemolytic strains of M. bovis, the mbx operon, including the adjacent M. bovis tolC orthologue, was flanked by approximately 700 bp imperfect repeats. Nonhaemolytic strains of M. bovis had only one or no such repeats, as well as ORFs identical to those flanking the repeats from haemolytic M. bovis. Two nonhaemolytic strains also contained ORFs with deduced amino acid sequence similarity to bacterial araJ genes. The G+C content of the mbxCABDtolC gene region was lower than the flanking regions. The genetic organization and G+C content of mbxCABDtolC genes, and flanking repeats in haemolytic M. bovis, as well as the presence or absence of flanking repeats in nonhaemolytic M. bovis, suggests that this RTX operon is located on a mobile genetic element, and supports the designation of this region as a pathogenicity island, which is believed to be the first such element demonstrated in M. bovis.

Amino acid sequence similarity between cytochrome f from a blue-green bacterium and algal chloroplasts

Nature ◽  
1975 ◽  
Vol 253 (5489) ◽  
pp. 285-288 ◽  
Author(s):  
R. P. AMBLER ◽  
R. G. BARTSCH
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Similarity ◽  
Cytochrome F ◽  
Amino Acid Sequence Similarity ◽  
Green Bacterium
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