scholarly journals The shdA Gene Is Restricted to Serotypes ofSalmonella enterica Subspecies I and Contributes to Efficient and Prolonged Fecal Shedding

2000 ◽  
Vol 68 (5) ◽  
pp. 2720-2727 ◽  
Author(s):  
Robert A. Kingsley ◽  
Karin van Amsterdam ◽  
Naomi Kramer ◽  
Andreas J. Bäumler
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Domestic Fowl ◽  
Shigella Flexneri ◽  
Open Reading Frame ◽  
Fecal Shedding ◽  
Reading Frame ◽  
K 12

ABSTRACT Little is known about factors which enable Salmonellaserotypes to circulate within populations of livestock and domestic fowl. We have identified a DNA region which is present inSalmonella serotypes commonly isolated from livestock and domestic fowl (S. enterica subspecies I) but absent from reptile-associated Salmonella serotypes (S. bongori and S. enterica subspecies II to VII). This DNA region was cloned from Salmonella serotype Typhimurium and sequence analysis revealed the presence of a 6,105-bp open reading frame, designated shdA, whose product's deduced amino acid sequence displayed homology to that of AIDA-I from diarrheagenicEscherichia coli, MisL of serotype Typhimurium, and IcsA ofShigella flexneri. The shdA gene was located adjacent to xseA at 52 min, in a 30-kb DNA region which is not present in Escherichia coli K-12. A serotype Typhimurium shdA mutant was shed with the feces in reduced numbers and for a shorter period of time compared to its isogenic parent. A possible role for the shdA gene during the expansion in host range of S. enterica subspecies I to include warm-blooded vertebrates is discussed.

scholarly journals Characteristics of a New Enantioselective Thermostable Dipeptidase from Brevibacillus borstelensis BCS-1 and Its Application to Synthesis of a d-Amino-Acid-Containing Dipeptide

2004 ◽  
Vol 70 (3) ◽  
pp. 1570-1575 ◽  
Author(s):  
Dae Heoun Baek ◽  
Jae Jun Song ◽  
Seok-Joon Kwon ◽  
Chung Park ◽  
Chang-Min Jung ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Open Reading Frame ◽  
Nucleotide Sequence Analysis ◽  
Reading Frame ◽  
E Coli ◽  
Specificity Constant ◽  
Optimal Ph

ABSTRACT A new thermostable dipeptidase gene was cloned from the thermophile Brevibacillus borstelensis BCS-1 by genetic complementation of the d-Glu auxotroph Escherichia coli WM335 on a plate containing d-Ala-d-Glu. Nucleotide sequence analysis revealed that the gene included an open reading frame coding for a 307-amino-acid sequence with an M r of 35,000. The deduced amino acid sequence of the dipeptidase exhibited 52% similarity with the dipeptidase from Listeria monocytogenes. The enzyme was purified to homogeneity from recombinant E. coli WM335 harboring the dipeptidase gene from B. borstelensis BCS-1. Investigation of the enantioselectivity (E) to the P1 and P1′ site of Ala-Ala revealed that the ratio of the specificity constant (k cat /Km ) for l-enantioselectivity to the P1 site of Ala-Ala was 23.4 � 2.2 [E = (k cat /Km ) l,d /(k cat /Km ) d,d ], while the d-enantioselectivity to the P1′ site of Ala-Ala was 16.4 � 0.5 [E = (k cat /Km ) l,d /(k cat /Km ) l,l ] at 55�C. The enzyme was stable up to 55�C, and the optimal pH and temperature were 8.5 and 65�C, respectively. The enzyme was able to hydrolyze l-Asp-d-Ala, l-Asp-d-AlaOMe, Z-d-Ala-d-AlaOBzl, and Z-l-Asp-d-AlaOBzl, yet it could not hydrolyze d-Ala-l-Asp, d-Ala-l-Ala, d-AlaNH2, and l-AlaNH2. The enzyme also exhibited β-lactamase activity similar to that of a human renal dipeptidase. The dipeptidase successfully synthesized the precursor of the dipeptide sweetener Z-l-Asp-d-AlaOBzl.

scholarly journals Outbreak of equid herpesvirus 1 abortions at the Arabian stud in Poland

2020 ◽  
Vol 16 (1) ◽  
Author(s):  
Karol Stasiak ◽  
Magdalena Dunowska ◽  
Jerzy Rola
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Neurological Disease ◽  
Open Reading Frame ◽  
Case Presentation ◽  
Reading Frame ◽  
Equid Herpesvirus ◽  
Herpesvirus 1 ◽  
Horizontal Spread

Abstract Background Equid herpesvirus 1 (EHV-1) infections are endemic worldwide, including Poland. Many are subclinical, but some are associated with respiratory disease, abortion, neonatal foal death, or neurological disease. We describe an outbreak of abortions in Arabian mares at a well-managed State stud farm in Poland. Case presentation Eight of 30 pregnant mares aborted and one gave birth to a weak foal that died within 72 h after birth. EHV-1 was isolated from all fetuses as well as from the diseased foal. All viruses belonged to the N752 variant based on the predicted open reading frame (ORF) 30 amino acid sequence. All were identical to each other and to previous EHV-1 viruses from the same stud based on the ORF68 sequence analysis. The outbreak coincided with the lapse in the routine yearly EHV-1/4 vaccinations of the mares. Conclusions Multiple abortion due to EHV-1 infection can occur in well-managed groups of horses. Reactivation of latent EHV-1 in one of the resident mares followed by a horizontal spread was considered the most likely explanation for the outbreak. Routine vaccination is an important part of a herd-heath program.

scholarly journals Cloning, Expression, and Sequence Analysis of the ORF4 Gene of the Porcine Reproductive and Respiratory Syndrome Virus MN-1b

1994 ◽  
Vol 6 (3) ◽  
pp. 293-296 ◽  
Author(s):  
Jimmy Kwang ◽  
Hyun Soo Kim ◽  
Han S. Joo
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequences ◽  
Open Reading Frame ◽  
Respiratory Syndrome Virus ◽  
European Isolate ◽  
Reading Frame ◽  
Orf4 Protein ◽  
Orf4 Gene

Porcine reproductive and respiratory syndrome virus (PRRSV) MN-1b strain open reading frame 4 (ORF4) has been cloned, sequenced, and expressed in Escherichia coli. The homologies of nucleotide and amino acid sequences between MN-1b (US isolate) and LV (European isolate) are 69% and 64%, respectively. The data also showed that ORF4 of MN-1b is 36 bases shorter than that of LV. Western blot analysis of expressed recombinant ORF4 protein reacted with 65% (26/40) of PRRSV-infected pig sera tested. These results demonstrated that ORF4 of PRRSV may not be a well-conserved region.

scholarly journals Monooxygenase-like sequence of a Rhodococcus equi gene conferring increased resistance to rifampin by inactivating this antibiotic.

1997 ◽  
Vol 41 (1) ◽  
pp. 218-221 ◽  
Author(s):  
S J Andersen ◽  
S Quan ◽  
B Gowan ◽  
E R Dabbs
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Phenolic Compounds ◽  
Amino Acid Sequence ◽  
Rhodococcus Equi ◽  
Open Reading Frame ◽  
Reading Frame ◽  
Low Level ◽  
Antibiotic Synthesis ◽  
Rifampin Resistance

A DNA clone from Rhodococcus equi conferring low-level rifampin resistance through the ability to inactivate this antibiotic via its decomposition was identified. The iri (inactivation of rifampin) gene consisted of an open reading frame of 1,437 bp encoding a 479-amino-acid sequence strongly resembling those of monooxygenases acting upon phenolic compounds or involved in polyketide antibiotic synthesis. When expressed in Escherichia coli, the gene conferred resistance to a > 50-micrograms/ml concentration of the drug.

scholarly journals Identification of the ubiD Gene on theEscherichia coli Chromosome

2000 ◽  
Vol 182 (21) ◽  
pp. 6243-6246 ◽  
Author(s):  
Haitao Zhang ◽  
George T. Javor
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Gene Product ◽  
Mutant Strain ◽  
Amino Acid Residue ◽  
Open Reading Frame ◽  
Reading Frame

ABSTRACT The open reading frame at 86.7 min on the Escherichia coli chromosome, “yigC,” complemented aubiD mutant strain, AN66, indicating that yigCis the ubiD gene. The gene product, a 497-amino-acid-residue protein, showed extensive homology to the UPF 00096 family of proteins in the Swiss-Prot database.

scholarly journals Plasmid-Encoded asp Operon Confers a Proton Motive Metabolic Cycle Catalyzed by an Aspartate-Alanine Exchange Reaction

2002 ◽  
Vol 184 (11) ◽  
pp. 2906-2913 ◽  
Author(s):  
Keietsu Abe ◽  
Fumito Ohnishi ◽  
Kyoko Yagi ◽  
Tasuku Nakajima ◽  
Takeshi Higuchi ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Expression Vector ◽  
Alcaligenes Faecalis ◽  
E Coli ◽  
Cell Extracts ◽  
Membrane Spanning ◽  
Metabolic Cycle

ABSTRACT Tetragenococcus halophila D10 catalyzes the decarboxylation of l-aspartate with nearly stoichiometric release of l-alanine and CO2. This trait is encoded on a 25-kb plasmid, pD1. We found in this plasmid a putative asp operon consisting of two genes, which we designated aspD and aspT, encoding an l-aspartate-β-decarboxylase (AspD) and an aspartate-alanine antiporter (AspT), respectively, and determined the nucleotide sequences. The sequence analysis revealed that the genes of the asp operon in pD1 were in the following order: promoter → aspD → aspT. The deduced amino acid sequence of AspD showed similarity to the sequences of two known l-aspartate-β-decarboxylases from Pseudomonas dacunhae and Alcaligenes faecalis. Hydropathy analyses suggested that the aspT gene product encodes a hydrophobic protein with multiple membrane-spanning regions. The operon was subcloned into the Escherichia coli expression vector pTrc99A, and the two genes were cotranscribed in the resulting plasmid, pTrcAsp. Expression of the asp operon in E. coli coincided with appearance of the capacity to catalyze the decarboxylation of aspartate to alanine. Histidine-tagged AspD (AspDHis) was also expressed in E. coli and purified from cell extracts. The purified AspDHis clearly exhibited activity of l-aspartate-β-decarboxylase. Recombinant AspT was solubilized from E. coli membranes and reconstituted in proteoliposomes. The reconstituted AspT catalyzed self-exchange of aspartate and electrogenic heterologous exchange of aspartate with alanine. Thus, the asp operon confers a proton motive metabolic cycle consisting of the electrogenic aspartate-alanine antiporter and the aspartate decarboxylase, which keeps intracellular levels of alanine, the countersubstrate for aspartate, high.

scholarly journals Serine and threonine catabolism in Saccharomyces cerevisiae: the CHA1 polypeptide is homologous with other serine and threonine dehydratases.

Genetics ◽  
1992 ◽  
Vol 131 (3) ◽  
pp. 531-539 ◽  
Author(s):  
C Bornaes ◽  
J G Petersen ◽  
S Holmberg
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Transcription Initiation ◽  
Open Reading Frame ◽  
Predicted Amino Acid Sequence ◽  
S1 Nuclease ◽  
Reading Frame ◽  
Threonine Dehydratase ◽  
Nuclease Mapping

Abstract The catabolic L-serine (L-threonine) dehydratase of Saccharomyces cerevisiae allows the yeast to grow on media with L-serine or L-threonine as sole nitrogen source. Previously we have cloned the CHA1 gene by complementation of a mutant, cha1, lacking the dehydratase activity. Here we present the DNA sequence of a 1,766-bp fragment of the CHA1 region encompassing an open reading frame of 1080 bp. Comparison of the predicted amino acid sequence of the CHA1 polypeptide with that of other serine/threonine dehydratases revealed several blocks of sequence homology. Thus, the amino acid sequence of rat liver serine dehydratase (SDH2) and the CHA1 polypeptide are 44% homologous allowing for conservative substitutions, while 36% similarity is found between the catabolic threonine dehydratase (tdcB) of Escherichia coli and the CHA1 protein. This strongly suggests that CHA1 is the structural gene for the yeast catabolic serine (threonine) dehydratase. S1-nuclease mapping of the CHA1 mRNA ends showed a major transcription initiation site corresponding to an untranslated leader of about 19 nucleotides, while a major polyadenylation site was located about 86 nucleotides downstream from the open reading frame. Furthermore, we have mapped the chromosomal position of the CHA1 gene to less than 0.5 kb centromere proximal to HML on the left arm of chromosome III.

scholarly journals Sequence Conservation of Glycerophosphodiester Phosphodiesterase among Treponema pallidum Strains

1999 ◽  
Vol 67 (6) ◽  
pp. 3168-3170 ◽  
Author(s):  
Caroline E. Cameron ◽  
Christa Castro ◽  
Sheila A. Lukehart ◽  
Wesley C. Van Voorhis
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Subunit Vaccine ◽  
Nucleotide Substitution ◽  
Restriction Site ◽  
Treponema Pallidum ◽  
Open Reading Frame ◽  
Reading Frame ◽  
Attractive Candidate ◽  
Glycerophosphodiester Phosphodiesterase

ABSTRACT Previous investigations have demonstrated that immunization withTreponema pallidum subsp. pallidumglycerophosphodiester phosphodiesterase significantly protects rabbits from subsequent treponeme challenge. In this report, we show that the glycerophosphodiester phosphodiesterase amino acid sequence is conserved among 12 strains from a total of five pathogenic treponemes. The invariant nature of this immunoprotective antigen makes it an attractive candidate for inclusion in a universal subunit vaccine against T. pallidum infection. In addition, these studies show a silent nucleotide substitution at position 579 of thegpd open reading frame which is consistently observed in the non-T. pallidum subsp. pallidum strains. This sequence alteration introduces a PleI restriction site in the nonsyphilis strains and thus allows genetic differentiation fromT. pallidum subsp. pallidum strains.

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