scholarly journals A Myristylated Membrane Protein Encoded by the Vaccinia Virus L1R Open Reading Frame Is the Target of Potent Neutralizing Monoclonal Antibodies

Virology ◽  
1995 ◽  
Vol 211 (1) ◽  
pp. 53-63 ◽  
Author(s):  
Elizabeth J. Wolffe ◽  
S. Vijaya ◽  
Bernard Moss
Keyword(s):  
Monoclonal Antibodies ◽  
Membrane Protein ◽  
Vaccinia Virus ◽  
Open Reading Frame ◽  
Reading Frame

scholarly journals Identification by Subtractive Hybridization of a Novel Insertion Sequence Specific for Virulent Strains ofPorphyromonas gingivalis

1999 ◽  
Vol 67 (11) ◽  
pp. 5621-5625 ◽  
Author(s):  
Koichi Sawada ◽  
Susumu Kokeguchi ◽  
Hiroshi Hongyo ◽  
Satoko Sawada ◽  
Manabu Miyamoto ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Subtractive Hybridization ◽  
Open Reading Frame ◽  
Specific Marker ◽  
Avirulent Strain ◽  
Target Sequence ◽  
Dna Fragments ◽  
Reading Frame

ABSTRACT Subtractive hybridization was employed to isolate specific genes from virulent Porphyromonas gingivalis strains that are possibly related to abscess formation. The genomic DNA from the virulent strain P. gingivalis W83 was subtracted with DNA from the avirulent strain ATCC 33277. Three clones unique to strain W83 were isolated and sequenced. The cloned DNA fragments were 885, 369, and 132 bp and had slight homology with only Bacillus stearothermophilus IS5377, which is a putative transposase. The regions flanking the cloned DNA fragments were isolated and sequenced, and the gene structure around the clones was revealed. These three clones were located side-by-side in a gene reported as an outer membrane protein. The three clones interrupt the open reading frame of the outer membrane protein gene. This inserted DNA, consisting of three isolated clones, was designated IS1598, which was 1,396 bp (i.e., a 1,158-bp open reading frame) in length and was flanked by 16-bp terminal inverted repeats and a 9-bp duplicated target sequence. IS1598 was detected inP. gingivalis W83, W50, and FDC 381 by Southern hybridization. All three P. gingivalis strains have been shown to possess abscess-forming ability in animal models. However, IS1598 was not detected in avirulent strains of P. gingivalis, including ATCC 33277. The IS1598 may interrupt the synthesis of the outer membrane protein, resulting in changes in the structure of the bacterial outer membrane. The IS1598 isolated in this study is a novel insertion element which might be a specific marker for virulent P. gingivalisstrains.

scholarly journals Human Coronavirus NL63 Open Reading Frame 3 encodes a virion-incorporated N-glycosylated membrane protein

2010 ◽  
Vol 7 (1) ◽  
pp. 6 ◽  
Author(s):  
Marcel A Müller ◽  
Lia van der Hoek ◽  
Daniel Voss ◽  
Oliver Bader ◽  
Dörte Lehmann ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Open Reading Frame ◽  
Human Coronavirus ◽  
Reading Frame

scholarly journals The apbE Gene Encodes a Lipoprotein Involved in Thiamine Synthesis in Salmonella typhimurium

1998 ◽  
Vol 180 (4) ◽  
pp. 885-891 ◽  
Author(s):  
Brian J. Beck ◽  
Diana M. Downs
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Salmonella Typhimurium ◽  
De Novo ◽  
Open Reading Frame ◽  
Thiamine Pyrophosphate ◽  
Gene Products ◽  
Reading Frame ◽  
Purine Pathway

ABSTRACT Thiamine pyrophosphate is an essential cofactor that is synthesized de novo in Salmonella typhimurium. The biochemical steps and gene products involved in the conversion of aminoimidazole ribotide (AIR), a purine intermediate, to the 4-amino-5-hydroxymethyl-2-methyl pyrimidine (HMP) moiety of thiamine have yet to be elucidated. We have isolated mutations in a new locus (Escherichia coli open reading frame designation yojK) at 49 min on the S. typhimurium chromosome. Two significant phenotypes associated with lesions in this locus (apbE) were identified. First,apbE purF double mutants require thiamine, specifically the HMP moiety. Second, in the presence of adenine, apbE single mutants require thiamine, specifically both the HMP and the thiazole moieties. Together, the phenotypes associated with apbEmutants suggest that flux through the purine pathway has a role in regulating synthesis of the thiazole moiety of thiamine and are consistent with ApbE being involved in the conversion of AIR to HMP. The product of the apbE gene was found to be a 36-kDa membrane-associated lipoprotein, making it the second membrane protein implicated in thiamine synthesis.

scholarly journals Vaccinia Virus WR Gene A5L Is Required for Morphogenesis of Mature Virions

1999 ◽  
Vol 73 (6) ◽  
pp. 4590-4599 ◽  
Author(s):  
Ollie Williams ◽  
Elizabeth J. Wolffe ◽  
Andrea S. Weisberg ◽  
Michael Merchlinsky
Keyword(s):  
Vaccinia Virus ◽  
Open Reading Frame ◽  
Reading Frame ◽  
Endogenous Gene ◽  
Late Protein ◽  
Full Complement ◽  
Immature Virion ◽  
Infected Cells ◽  
Synthesis And Processing ◽  
Vaccinia Virion

ABSTRACT The vaccinia virus WR A5L open reading frame (corresponding to open reading frame A4L in vaccinia virus Copenhagen) encodes an immunodominant late protein found in the core of the vaccinia virion. To investigate the role of this protein in vaccinia virus replication, we have constructed a recombinant virus, vA5Li, in which the endogenous gene has been deleted and an inducible copy of the A5 gene dependent on isopropyl-β-d-thiogalactopyranoside (IPTG) for expression has been inserted into the genome. In the absence of inducer, the yield of infectious virus was dramatically reduced. However, DNA synthesis and processing, viral protein expression (except for A5), and early stages in virion formation were indistinguishable from the analogous steps in a normal infection. Electron microscopy revealed that the major vaccinia virus structural form present in cells infected with vA5Li in the absence of inducer was immature virions. Viral particles were purified from vA5Li-infected cells in the presence and absence of inducer. Both particles contained viral DNA and the full complement of viral proteins, except for A5, which was missing from particles prepared in the absence of inducer. The particles prepared in the presence of IPTG were more infectious than those prepared in its absence. The A5 protein appears to be required for the immature virion to form the brick-shaped intracellular mature virion.

scholarly journals Vaccinia Virus Nicking-Joining Enzyme Is Encoded by K4L (VACWR035)

2005 ◽  
Vol 79 (24) ◽  
pp. 15084-15090 ◽  
Author(s):  
Dawn Eckert ◽  
Ollie Williams ◽  
Clement A. Meseda ◽  
Michael Merchlinsky
Keyword(s):  
Vaccinia Virus ◽  
Recombinant Virus ◽  
Nuclease Activity ◽  
Open Reading Frames ◽  
Open Reading Frame ◽  
Virus Protein ◽  
Gene Encoding ◽  
Independent Manner ◽  
Reading Frame ◽  
Cross Links

ABSTRACT Vaccinia virus encodes an enzyme with DNA modifying activity that cleaves and inefficiently cross-links cruciformic DNA. This enzyme is contained within the virion, expressed at late times postinfection, and processes DNA in an energy-independent, Mg2+ ion-independent manner. Viral nuclease activity was measured in extracts from cells infected with well-defined viral mutants. Since some viral extracts lacked nuclease activity, the gene encoding the activity was postulated to be one of the open reading frames absent in the viruses lacking activity. Inducible expression of each candidate open reading frame revealed that only the gene VACWR035, or K4L, was required for nuclease activity. A recombinant virus missing only the open reading frame for K4L lacked nuclease activity. Extracts from a recombinant virus expressing K4L linked to a FLAG polypeptide were able to cleave and cross-link cruciformic DNA. There were no significant differences between the virus lacking K4L and wild-type vaccinia virus WR with respect to infectivity, growth characteristics, or processing of viral replicative intermediate DNA, including both telomeric and cross-linked forms. Purification of the K4L FLAG polypeptide expressed in bacteria yielded protein containing nicking-joining activity, implying that K4L is the only vaccinia virus protein required for the nicking-joining enzymatic activity.

scholarly journals Hypothetical Protein Cpn0308 Is Localized in the Chlamydia pneumoniae Inclusion Membrane

2006 ◽  
Vol 75 (1) ◽  
pp. 497-503 ◽  
Author(s):  
Jianhua Luo ◽  
Tianjun Jia ◽  
Rhonda Flores ◽  
Ding Chen ◽  
Guangming Zhong
Keyword(s):  
Membrane Protein ◽  
Fusion Proteins ◽  
Chlamydia Pneumoniae ◽  
Hypothetical Protein ◽  
Open Reading Frame ◽  
Inclusion Membrane ◽  
Reading Frame ◽  
Antibody Staining ◽  
Infected Cells ◽  
Antibody Labeling

ABSTRACT The hypothetical protein encoded by Chlamydia pneumoniae open reading frame cpn0308 was detected in inclusion membranes of C. pneumoniae-infected cells using antibodies raised with Cpn0308 fusion proteins. The anti-Cpn0308 antibodies did not cross-react with IncA, a known C. pneumoniae inclusion membrane protein, although the anti-Cpn0308 antibody staining overlapped with the anti-IncA antibody labeling. The labeling of the inclusion membrane by the anti-Cpn0308 antibody was specifically blocked by the Cpn0308 but not IncA fusion proteins. The Cpn0308 antigen was detectable 24 h after infection and remained in the inclusion membrane throughout the infection course.

Sign in / Sign up

Export Citation Format

Share Document