Department of Microbial and Molecular Pathogenesis, Texas A&M Health Science Center College of Medicine, Bryan, Texas 77807–3260, USA.
- Erin J. van Schaik,
- Chen Chen,
- Katja Mertens,
- Mary M. Weber &
- James E. Samuel
Present address: Friedrich Loeffler Institute, Federal Research Institute for Animal Health, Institute of Bacterial Infections and Zoonoses, Naumburger Str. 96a, 07743 Jena, Germany.
- Katja Mertens
Competing interests statement
The authors declare no competing interests.
Erin J. van Schaik
Erin J. van Schaik completed her Ph.D. at the University of Alberta in Canada studying Pseudomonas aeruginosa type IV pili and was a postdoctoral fellow in the laboratory of Donald Woods at the University of Calgary, Canada, where she studied the pathogenic mechanisms of Burkholderia pseudomallei during acute and chronic infections. She is currently a postdoctoral fellow in the laboratory of James Samuel at the Texas A&M Health Science Center College of Medicine, Bryan, USA, where she studies the role of type II secretion in the pathogenesis of Coxiella burnetii.
Chen Chen completed his Ph.D. at the Texas A&M Health Science Center College of Medicine, Bryan, USA, in James Samuel's laboratory, where he worked on identifying an array of type IV secretion substrates encoded by Coxiella burnetii and defining components of protective immunity against Q fever in humans and animal models of infection. He is currently a postdoctoral fellow in the laboratory of Daniel Portnoy at the University of California, Berkley, USA.
Katja Mertens completed her Ph.D. at the University of Bayreuth, Germany, working on polysaccharide expression and serotype association in Klebsiella and Raoultella strain serology. She joined the laboratory of James Samuel at the Texas A&M Health Science Center College of Medicine, Bryan, USA, as a postdoctoral fellow and progressed to the rank of Assistant Professor while developing tools for genetic exchange and lipopolyaccharide biosynthesis for Coxiella burnetii. She is currently a scientist at the Friedrich-Loeffler-Institute, Jena, Germany.
Mary M. Weber
Mary M. Weber completed her M.S. at Texas State University, San Marcos, USA, in the laboratory of Robert McLean working on biofilm formation and stress responses in Escherichia coli. She joined the laboratory of Jim Samuel at the Texas A&M Health Science Center College of Medicine, Bryan, USA, in 2009 and currently serves as a pre-doctoral fellow. Her dissertation projects involve elucidating the role of type IV secretion-dependent effectors in host cell manipulation and virulence.
James E. Samuel
James E. Samuel obtained his Ph.D. for his work characterizing fundamental genetic elements of Coxiella burnetii and their application for the differentiation of strains from various clinical and environmental reservoirs. The concepts derived from these studies have been supported by experiments more than 20 years later, and the differences in virulence potential between clinical isolates that lead to acute and chronic manifestations of disease have now begun to be established. His research group at the Texas A&M Health Science Center College of Medicine, Bryan, USA, works on components of the host response to infection, for the design of a new generation of vaccines, and on broad questions of molecular pathogenesis, including the role of a large variety of type IV secretion effectors. James E. Samuel's homepage.
- Axenic culture media
Media used for the growth of intracellular bacteria in the absence of host cells.
- Category B select agent
An infectious disease agent of the second highest priority, as defined by the US CDC guidelines for potential misuse. These agents are usually readily transmitted by aerosol, are stable in the environment and cause moderate morbidity and low mortality.
- BL3 containment
A level of biocontainment that includes a separation from general traffic areas by double doors, airlocks and negative air flow. Access is limited to trained personnel and requires users to wear personal protective equipment. All research activities with potential exposure of the agent to the atmosphere are conducted within biosafety cabinets.
A highly conserved family of heterodimeric surface glycoproteins involved in binding to extracellular matrix components such as fibronectin and vitronectin through arginine-glycine-aspartic acid (RGD) domains.
- BL2 containment
A level of biocontainment that involves the use of standard laboratory space in which work using an infectious agent is carried out within a biosafety cabinet.
- SRC tyrosine kinases
A family of kinases that was originally identified through homology to Rous sarcoma virus oncogene v-src and is involved in signal transduction from cellular receptors.
Loss of weight, fatigue and weakness that are associated with severe inflammatory disease and cannot be reversed by nutritional supplementation.
- Himar1-based transposon system
A eukaryotic horn fly element that is extensively used to create mutations in bacteria and relies on only an AT dinucleotide for insertion.
- C. burnetii str. Nine Mile I
The original Coxiella burnetii strain isolated from ticks in 1935. This strain was later serially passaged in embryonated hen eggs and guinea pigs to obtain the avirulent isolate C. burnetii str. Nine Mile II.
- Two-component regulatory system
A bacterial signal transduction system involving a sensor kinase that responds to an environmental stimulus by phosphorylating a response regulator, which controls the transcription of downstream genes.
- Insertion sequences
Mobile genetic elements consisting of short inverted repeats flanking one or more ORFs.
- Ankyrin repeats
Eukaryotic protein domains consisting of repeating segments of 33 amino acids that form a helix–turn–helix motif and mediate protein–protein interactions. These domains are some of the most commonly found domains in eukaryotic proteins.
- Coiled-coil domains
Structural motifs that are found in proteins and consist of 2–5 α-helices wrapped around each other in a left-handed manner to form a superhelix.
- Tetratricopeptide repeats
Structural motifs that mediate protein–protein interactions and are composed of a degenerate ~34 amino acid sequence that is often arranged in a tandem array.
- F-box domains
Structural motifs composed of approximately 50 amino acids and that contain tryptophan-aspartic acid repeats. These domains function as protein–protein interaction domains. F-box proteins were first characterized as components of ubiquitin ligase complexes.
- Fic domains
(Filamentation induced by cyclic AMP domains). Protein domains that mediate ampylation of proteins and regulate protein function.