Roles for motility in bacterial–host interactions

Ottemann, Karen M.; Miller, Jeff F.

doi:10.1046/j.1365-2958.1997.4281787.x

Cited by 294 publications

(224 citation statements)

References 60 publications

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“…At the biochemical level, inactivation of the ppk gene was confirmed by a loss of PPK activity and a decrease in poly P accumulation (data not shown). Because motility is intimately involved in survival, symbiosis, and virulence of bacteria (9)(10)(11), the effects of the mutation on various forms of motility were examined.…”

Section: Resultsmentioning

confidence: 99%

“…These various forms of surface motility enable bacteria to establish symbiotic and pathogenic associations with plants and animals (9)(10)(11). Potential benefits of motility include increased efficiency of nutrient acquisition, avoidance of toxic substances, ability to translocate to preferred hosts and access to optimal colonization sites within them, and dispersal in the environment during the course of transmission.…”

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confidence: 99%

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Inorganic polyphosphate is needed for swimming, swarming, and twitching motilities of Pseudomonas aeruginosa

Rashid

Kornberg

2000

Proc. Natl. Acad. Sci. U.S.A.

739

598

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Polyphosphate kinase (PPK), encoded by the ppk gene, is the principal enzyme in many bacteria for the synthesis of inorganic polyphosphate (poly P) from ATP. A knockout mutant in the ppk gene of Pseudomonas aeruginosa PAO1 is impaired in flagellar swimming motility on semisolid agar plates. The mutant is deficient in type IV pili-mediated twitching motility and in a ''swarming motility'' previously unobserved in P. aeruginosa. In swarming cultures, the polar monotrichous bacteria have differentiated into elongated and polar multitrichous cells that navigate the surface of solid media. All of the motility defects in the ppk mutant could be complemented by a plasmid harboring the ppk gene. Because bacterial motility is often crucial for their survival in a natural environment and for systemic infection inside a host, the dependence for motility on PPK reveals important roles for poly P in diverse processes such as biofilm formation, symbiosis, and virulence.I norganic polyphosphate (poly P) is a linear chain of tens or many hundreds of phosphate residues linked by high-energy phosphoanhydride bonds. It is found in every cell in nature: bacterial, archaeal, fungal, protozoan, plant, and animal (1, 2). Poly P has numerous and varied biological functions depending on where it is (species, cell, or subcellular compartment) and when it is needed. Among these functions are substitution for ATP in kinase reactions; reservoir of phosphate; chelation of divalent metals; capsule of bacteria; and regulatory roles in growth, development, stress, and deprivation (1, 2). In our studies of Escherichia coli, the most significant function observed thus far is its regulatory role in adapting to nutritional stringencies and environmental stresses, and for survival in the stationary phase of growth (3). This role has been inferred from the behavior of mutant cells lacking polyphosphate kinase (PPK), the enzyme responsible for the synthesis of poly P from ATP (4).Motility is arguably one of the most impressive features in microbial physiology. Movement in aqueous environments by swimming or along surfaces by using different modes of translocation has been classified into several distinct forms (5). Swimming on a surface takes place when the fluid film is sufficiently thick and the micromorphological pattern is unorganized. When the fluid layer on a surface is relatively thin, the swimming bacteria become elongated and hyperflagellated and move in a coordinated manner known as ''swarming'' (5-7). Twitching motility is another form of translocation on a solid surface in which the micromorphological pattern is less organized than in swarming (5, 8). Among these three modes of surface translocation, swimming and swarming depend on flagella, whereas twitching depends on type IV pili (5).These various forms of surface motility enable bacteria to establish symbiotic and pathogenic associations with plants and animals (9-11). Potential benefits of motility include increased efficiency of nutrient acquisition, avoidance of toxic substances, ab...

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Inorganic polyphosphate is needed for swimming, swarming, and twitching motilities of Pseudomonas aeruginosa

Rashid

Kornberg

2000

Proc. Natl. Acad. Sci. U.S.A.

739

598

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“…Flagella play a role in bacterial adaptation to environmental conditions and have often been associated with the virulence of various pathogens (Ottemann & Miller, 1997). The flagellar system of Escherichia coli and Salmonella typhimurium is encoded by over 40 genes (Aldridge & Hughes, 2002).…”

Section: Introductionmentioning

confidence: 99%

Integration host factor (IHF) mediates repression of flagella in enteropathogenic and enterohaemorrhagic Escherichia coli

et al. 2003

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“…In many pathogenic species, they also act as virulence factors because motility is required to reach the primary site of infection and thereby establish the first step of a bacterial infection (2,3). Flagella assembly involves more than 50 proteins and is a hierarchical process (1,4).…”

mentioning

confidence: 99%

The crystal structure of the third signal-recognition particle GTPase FlhF reveals a homodimer with bound GTP

Bange

Petzold

Wild

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

101

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Flagella are well characterized as the organelles of locomotion and allow bacteria to react to environmental changes. The assembly of flagella is a multistep process and relies on a complex type III export machinery located in the cytoplasmic membrane. The FlhF protein is essential for the placement and assembly of polar flagella and has been classified as a signal-recognition particle (SRP)-type GTPase. SRP GTPases appeared early in evolution and form a unique subfamily within the guanine nucleotide binding proteins with only three members: the signal sequence-binding protein SRP54, the SRP receptor FtsY, and FlhF. We report the crystal structures of FlhF from Bacillus subtilis in complex with GTP and GMPPNP. FlhF shares SRP GTPase-specific features such as the presence of an N-terminal ␣-helical domain and the I-box insertion. It forms a symmetric homodimer sequestering a composite active site that contains two head-to-tail arranged nucleotides similar to the heterodimeric SRP-targeting complex. However, significant differences to the GTPases of SRP and the SRP receptor include the formation of a stable homodimer with GTP as well as severe modifications and even the absence of motifs involved in regulation of the other two SRP GTPases. Our results provide insights into SRP GTPases and their roles in two fundamentally different protein-targeting routes that both rely on efficient protein delivery to a secretion channel.flagellum ͉ protein translocation ͉ x-ray structure analysis ͉ protein targeting

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Roles for motility in bacterial–host interactions

Cited by 294 publications

References 60 publications

Inorganic polyphosphate is needed for swimming, swarming, and twitching motilities of Pseudomonas aeruginosa

Inorganic polyphosphate is needed for swimming, swarming, and twitching motilities of Pseudomonas aeruginosa

Integration host factor (IHF) mediates repression of flagella in enteropathogenic and enterohaemorrhagic Escherichia coli

The crystal structure of the third signal-recognition particle GTPase FlhF reveals a homodimer with bound GTP

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