scholarly journals Cloning and Characterization of a Gene Encoding the Major Surface Protein of the Bacterial EndosymbiontWolbachia pipientis

1998 ◽  
Vol 180 (9) ◽  
pp. 2373-2378 ◽  
Author(s):  
Henk R. Braig ◽  
Weiguo Zhou ◽  
Stephen L. Dobson ◽  
Scott L. O’Neill
Keyword(s):  
Molecular Mechanisms ◽  
Cytoplasmic Incompatibility ◽  
Surface Protein ◽  
Gene Encoding ◽  
Developmental Abnormalities ◽  
Intracellular Symbiont ◽  
Different Strains ◽  
Major Surface ◽  
High Level

ABSTRACT The maternally inherited intracellular symbiont Wolbachia pipientis is well known for inducing a variety of reproductive abnormalities in the diverse arthropod hosts it infects. It has been implicated in causing cytoplasmic incompatibility, parthenogenesis, and the feminization of genetic males in different hosts. The molecular mechanisms by which this fastidious intracellular bacterium causes these reproductive and developmental abnormalities have not yet been determined. In this paper, we report on (i) the purification of one of the most abundantly expressed Wolbachia proteins from infected Drosophila eggs and (ii) the subsequent cloning and characterization of the gene (wsp) that encodes it. The functionality of the wsp promoter region was also successfully tested in Escherichia coli. Comparison of sequences of this gene from different strains of Wolbachiarevealed a high level of variability. This sequence variation correlated with the ability of certain Wolbachia strains to induce or rescue the cytoplasmic incompatibility phenotype in infected insects. As such, this gene will be a very useful tool forWolbachia strain typing and phylogenetic analysis, as well as understanding the molecular basis of the interaction ofWolbachia with its host.

A gene encoding a 69-kilodalton major surface protein of Giardia intestinalis trophozoites

1993 ◽  
Vol 58 (2) ◽  
pp. 247-257 ◽  
Author(s):  
Peter L. Ey ◽  
KumKum Khanna ◽  
Paul A. Manning ◽  
Graham Mayrhofer
Keyword(s):  
Surface Protein ◽  
Giardia Intestinalis ◽  
Gene Encoding ◽  
Major Surface Protein ◽  
Major Surface

scholarly journals Characterization of Multidrug-Resistant Escherichia coli Isolates from Animals Presenting at a University Veterinary Hospital

2011 ◽  
Vol 77 (20) ◽  
pp. 7104-7112 ◽  
Author(s):  
Maria Karczmarczyk ◽  
Yvonne Abbott ◽  
Ciara Walsh ◽  
Nola Leonard ◽  
Séamus Fanning
Keyword(s):  
Escherichia Coli ◽  
Molecular Mechanisms ◽  
Gene Array ◽  
Multidrug Resistant ◽  
Genetic Determinants ◽  
Gene Encoding ◽  
Content Type ◽  
E Coli ◽  
Class 1

ABSTRACTIn this study, we examined molecular mechanisms associated with multidrug resistance (MDR) in a collection ofEscherichia coliisolates recovered from hospitalized animals in Ireland. PCR and DNA sequencing were used to identify genes associated with resistance. Class 1 integrons were prevalent (94.6%) and contained gene cassettes recognized previously and implicated mainly in resistance to aminoglycosides, β-lactams, and trimethoprim (aadA1,dfrA1-aadA1,dfrA17-aadA5,dfrA12-orfF-aadA2,blaOXA-30-aadA1,aacC1-orf1-orf2-aadA1,dfr7). Class 2 integrons (13.5%) contained thedfrA1-sat1-aadA1gene array. The most frequently occurring phenotypes included resistance to ampicillin (97.3%), chloramphenicol (75.4%), florfenicol (40.5%), gentamicin (54%), neomycin (43.2%), streptomycin (97.3%), sulfonamide (98.6%), and tetracycline (100%). The associated resistance determinants detected includedblaTEM,cat,floR,aadB,aphA1,strA-strB,sul2, andtet(B), respectively. TheblaCTX-M-2gene, encoding an extended-spectrum β-lactamase (ESβL), andblaCMY-2, encoding an AmpC-like enzyme, were identified in 8 and 18 isolates, respectively. The mobility of the resistance genes was demonstrated using conjugation assays with a representative selection of isolates. High-molecular-weight plasmids were found to be responsible for resistance to multiple antimicrobial compounds. The study demonstrated that animal-associated commensalE. coliisolates possess a diverse repertoire of transferable genetic determinants. Emergence of ESβLs and AmpC-like enzymes is particularly significant. To our knowledge, theblaCTX-M-2gene has not previously been reported in Ireland.

scholarly journals Characterization of the Mycobacterium tuberculosis erp gene encoding a potential cell surface protein with repetitive structures

Microbiology ◽  
1995 ◽  
Vol 141 (9) ◽  
pp. 2123-2130 ◽  
Author(s):  
F.-X. Berthet ◽  
J. Rauzier ◽  
E. M. Lim ◽  
W. Philipp ◽  
B. Gicquel ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Cell Surface ◽  
Surface Protein ◽  
Cell Surface Protein ◽  
Gene Encoding

scholarly journals Characterization of Anaplasma marginale Isolated from North American Bison

2003 ◽  
Vol 69 (8) ◽  
pp. 5001-5005 ◽  
Author(s):  
José de la Fuente ◽  
Elizabeth J. Golsteyn Thomas ◽  
Ronald A. Van Den Bussche ◽  
Robert G. Hamilton ◽  
Elaine E. Tanaka ◽  
...  
Keyword(s):  
New World ◽  
Surface Protein ◽  
Anaplasma Marginale ◽  
The United States ◽  
Bison Bison ◽  
Infected Cattle ◽  
Major Surface Protein ◽  
The World ◽  
Major Surface

ABSTRACT Anaplasma marginale (Rickettsiales: Anaplasmataceae), a tick-borne pathogen of cattle, is endemic in tropical and subtropical regions of the world. Although serologic tests have identified American bison, Bison bison, as being infected with A. marginale, the present study was undertaken to confirm A. marginale infection and to characterize isolates obtained from naturally infected bison in the United States and Canada. Major surface protein (MSP1a and MSP4) sequences of bison isolates were characterized in comparison with New World cattle isolates. Blood from one U.S. bison was inoculated into a susceptible, splenectomized calf, which developed acute anaplasmosis, demonstrating infectivity of this A. marginale bison isolate for cattle. The results of this study showed that these A. marginale isolates obtained from bison were similar to ones from naturally infected cattle.

scholarly journals Characterization of Major Surface Glycoprotein Genes of Human Pneumocystis carinii and High-Level Expression of a Conserved Region

1998 ◽  
Vol 66 (9) ◽  
pp. 4268-4273 ◽  
Author(s):  
Qin Mei ◽  
Ross E. Turner ◽  
Vivian Sorial ◽  
Diane Klivington ◽  
C. William Angus ◽  
...  
Keyword(s):  
Genomic Library ◽  
Pneumocystis Carinii ◽  
Surface Glycoprotein ◽  
High Level Expression ◽  
Serum Samples ◽  
Major Surface Glycoprotein ◽  
Adult Humans ◽  
Major Surface ◽  
High Level

ABSTRACT To facilitate studies of Pneumocystis cariniiinfection in humans, we undertook to better characterize and to express the major surface glycoprotein (MSG) of human P. carinii, an important protein in host-pathogen interactions. Seven MSG genes were cloned from a single isolate by PCR or genomic library screening and were sequenced. The predicted proteins, like rat MSGs, were closely related but unique variants, with a high level of conservation among cysteine residues. A conserved immunodominant region (of approximately 100 amino acids) near the carboxy terminus was expressed at high levels in Escherichia coli and used in Western blot studies. All 49 of the serum samples, which were taken from healthy controls as well as from patients with and withoutP. carinii pneumonia, were reactive with this peptide by Western blotting, supporting the hypothesis that most adult humans have been infected with P. carinii at some point. This recombinant MSG fragment, which is the first human P. carinii antigen available in large quantities, may be a useful reagent for investigating the epidemiology of P. cariniiinfection in humans.

scholarly journals Development of a Multivalent ISCOM Vaccine against Anaplasmosis

1993 ◽  
Author(s):  
Guy H. Palmer ◽  
Eugene Pipano ◽  
Terry F. McElwain ◽  
Varda Shkap ◽  
Donald P. Knowles, Jr.
Keyword(s):  
T Lymphocytes ◽  
Outer Membrane ◽  
Membrane Surface ◽  
Surface Protein ◽  
The United States ◽  
Surface Proteins ◽  
Efficient Production ◽  
Major Surface ◽  
Homologous Challenge

Anaplasmosis is an arthropod+borne disease of cattle caused by the rickettsia Anaplasma marginale and an impediment to efficient production of healthy livestock in both Israel and the United States. Our research focuses on development of a recombinant membrane surface protein (MSP) immunogen to replace current vaccines derived from the blood of infected cattle. The risk of widespread transmission of both known and newly emergent pathogens has prevented licensure of live blood-based vaccines in the U.S. and is a major concern for their continued use in Israel. Briefly, we accomplished the following in our BARD supported research: i) characterization of the intramolecular and intermolecular relationships of the native Major Surface Proteins (MSP) in the outer membrane; ii) expression, purification, and epitope characterization of the recombinant MSP-2, MSP-3, MSP-4, and MSP-5 proteins required to construct the recombinant ISCOM; iii) demonstration that the outer membrane-Quil A induces CD4+ T lymphocytes specific for the outer membrane polypeptides; iv) identification of CD4+ T lymphocytes that recognize outer membrane polypeptide epitopes conserved among other wise antigenically distinct strains; v) determination that immunization with the outer membrane-Quil A construct does not affect the ability of ticks to acquire or transmit A. marginale; and vi) demonstration that the outer membrane-Quil A construct induces complete protection against rickettsemia upon homologous challenge and significant protection against challenge with antigenically distinct strains, including tick transmission. Importantly, the level of protection against homologous challenge in the MSP vaccinates was comparable to that induced by live blood-based vaccines and demonstrates that development of a new generation of vaccines is feasible.

Characterization of Major Surface Glycoprotein Genes of Human Pneumocystis carinii and High-Level Expression of a Conserved Region

1998 ◽  
Vol 66 (9) ◽  
pp. 4268-4273
Author(s):  
Qin Mei ◽  
Ross E. Turner ◽  
Vivian Sorial ◽  
Diane Klivington ◽  
C. William Angus ◽  
...  
Keyword(s):  
Pneumocystis Carinii ◽  
Surface Glycoprotein ◽  
High Level Expression ◽  
Major Surface Glycoprotein ◽  
Conserved Region ◽  
Major Surface ◽  
High Level

scholarly journals Characterization of a Gene Encoding an Acetylase Required for Pyoverdine Synthesis in Pseudomonas aeruginosa

2006 ◽  
Vol 188 (8) ◽  
pp. 3149-3152 ◽  
Author(s):  
Iain L. Lamont ◽  
Lois W. Martin ◽  
Talia Sims ◽  
Amy Scott ◽  
Mary Wallace
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Molecular Basis ◽  
Type Ii ◽  
Gene Encoding ◽  
Different Strains ◽  
Pyoverdine Synthesis

ABSTRACT Strains of Pseudomonas aeruginosa secrete one of three pyoverdine siderophores (types I to III). We have characterized a gene, pvdY II (for the pvdY gene present in type II P. aeruginosa strains), that is only present in strains that make type II pyoverdine. A mutation in pvdY II prevented pyoverdine synthesis. Bioinformatic, genetic, and biochemical approaches indicate that the PvdYII enzyme catalyzes acetylation of hydroxyornithine. Expression of pvdY II is repressed by the presence of iron and upregulated by the presence of type II pyoverdine. Characterization of pvdY II provides insights into the molecular basis for production of different pyoverdines by different strains of P. aeruginosa.

scholarly journals Identification and Characterization of a Linear-Plasmid-Encoded Factor H-Binding Protein (FhbA) of the Relapsing Fever Spirochete Borrelia hermsii

2004 ◽  
Vol 186 (9) ◽  
pp. 2612-2618 ◽  
Author(s):  
Kelley M. Hovis ◽  
John V. McDowell ◽  
LaToya Griffin ◽  
Richard T. Marconi
Keyword(s):  
Molecular Mechanisms ◽  
Binding Protein ◽  
Genetic Locus ◽  
Factor H ◽  
Linear Plasmid ◽  
Relapsing Fever ◽  
Gene Encoding ◽  
Borrelia Hermsii ◽  
Identification And Characterization

ABSTRACT In North America, tick-borne relapsing fever (TBRF) is caused by the spirochete species Borrelia hermsii, Borrelia parkeri, and Borrelia turicatae. We previously demonstrated that some isolates of B. hermsii and B. parkeri are capable of binding factor H and that cell-bound factor H can participate in the factor I-mediated cleavage of C3b. Isolates that bound factor H expressed a factor H-binding protein (FHBP) that we estimated to be approximately 19 to 20 kDa in size and thus, pending further characterization, temporarily designated FHBP19. Until this report, none of the FHBPs of the TBRF spirochetes had been characterized. Here we have recovered the gene encoding the FHBP of B. hermsii YOR from a lambda ZAP II library and determined its sequence. The gene encodes a full-length protein of 22.7 kDa, which after processing is predicted to be 20.5 kDa. This protein, which we redesignate factor H-binding protein A (FhbA), is unique to B. hermsii. Two-dimensional pulsed-field gel electrophoresis and hybridization analyses revealed that the B. hermsii gene encoding FhbA is a single genetic locus that maps to a linear plasmid of approximately 220 kb. The general properties of FhbA were also assessed. The protein was found to be surface exposed and lipidated. Analysis of the antibody response to FhbA in infected mice revealed that it is antigenic during infection, indicating expression during infection. The identification and characterization of FhbA provides further insight into the molecular mechanisms of pathogenesis of the relapsing fever spirochetes.

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