Dataset Information

Directed Binding of Gliding Bacterium, Mycoplasma mobile, Shown by Detachment Force and Bond Lifetime.

ABSTRACT:

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Mycoplasma mobile, a fish-pathogenic bacterium, features a protrusion that enables it to glide smoothly on solid surfaces at a velocity of up to 4.5 µm s(-1) in the direction of the protrusion. M. mobile glides by a repeated catch-pull-release of sialylated oligosaccharides fixed on a solid surface by hundreds of 50-nm flexible "legs" sticking out from the protrusion. This gliding mechanism may be explained by a possible directed binding of each leg with sialylated oligosaccharides, by which the leg can be detached more easily forward than backward. In the present study, we used a polystyrene bead held by optical tweezers to detach a starved cell at rest from a glass surface coated with sialylated oligosaccharides and concluded that the detachment force forward is 1.6- to 1.8-fold less than that backward, which may be linked to a catch bond-like behavior of the cell. These results suggest that this directed binding has a critical role in the gliding mechanism.

Importance

Mycoplasma species are the smallest bacteria and are parasitic and occasionally commensal, as represented by Mycoplasma pneumoniae, which causes so-called "walking pneumonia" in humans. Dozens of species glide on host tissues, always in the direction of the characteristic cellular protrusion, by novel mechanisms. The fastest species, Mycoplasma mobile, catches, pulls, and releases sialylated oligosaccharides (SOs), which are common targets among influenza viruses, by means of a specific receptor based on the energy of ATP hydrolysis. Here, force measurements made with optical tweezers revealed that the force required to detach a cell from SOs is smaller forward than backward along the gliding direction. The directed binding should be a clue to elucidate this novel motility mechanism.

SUBMITTER: Tanaka A

PROVIDER: S-EPMC4937208 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature

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Publications

Directed Binding of Gliding Bacterium, Mycoplasma mobile, Shown by Detachment Force and Bond Lifetime.

Tanaka Akihiro A Nakane Daisuke D Mizutani Masaki M Nishizaka Takayuki T Miyata Makoto M

mBio 20160628 3

<h4>Unlabelled</h4>Mycoplasma mobile, a fish-pathogenic bacterium, features a protrusion that enables it to glide smoothly on solid surfaces at a velocity of up to 4.5 µm s(-1) in the direction of the protrusion. M. mobile glides by a repeated catch-pull-release of sialylated oligosaccharides fixed on a solid surface by hundreds of 50-nm flexible "legs" sticking out from the protrusion. This gliding mechanism may be explained by a possible directed binding of each leg with sialylated oligosaccha ...[more]

PMID: 27353751

Similar Datasets

Project description:Mycoplasma mobile is a fish pathogen that glides on solid surfaces by means of its own gliding machinery composed of internal and surface structures. In the present study, we focused on the function and structure of Gli123, a surface protein that is essential for the localization of other surface proteins. The amino acid sequence of Gli123, which is 1,128 amino acids long, contains lipoprotein-specific repeats. We isolated the native Gli123 protein from M. mobile cells and a recombinant protein, rGli123, from Escherichia coli. The isolated rGli123 complemented a nonbinding and nongliding mutant of M. mobile that lacked Gli123. Circular dichroism and rotary-shadowing electron microscopy (EM) showed that rGli123 has a structure that is not significantly different from that of the native protein. Rotary-shadowing EM suggested that Gli123 adopts two distinct globular and rod-like structures, depending on the ionic strength of the solution. Negative-staining EM coupled with single-particle analysis revealed that Gli123 forms a globular structure featuring a small protrusion with dimensions of approximately 15.7, 14.7, and 14.1 nm for the "height," major axis and minor axis, respectively. Small-angle X-ray scattering analyses indicated a rod-like structure composed of several tandem globular domains with total dimensions of approximately 34 nm in length and 6 nm in width. Both molecular structures were suggested to be dimers, based on the predicted molecular size and structure. Gli123 may have evolved by multiplication of repeating lipoprotein units and acquired a role for Gli521 and Gli349 assembly. IMPORTANCE Mycoplasmas are pathogenic bacteria that are widespread in animals. They are characterized by small cell and genome sizes but are equipped with unique abilities for infection, such as surface variation and gliding. Here, we focused on a surface-localizing protein named Gli123 that is essential for Mycoplasma mobile gliding. This study suggested that Gli123 undergoes drastic conformational changes between its rod-like and globular structures. These changes may be caused by a repetitive structure common in the surface proteins that is responsible for the modulation of the cell surface structure and related to the assembly process for the surface gliding machinery. An evolutionary process for surface proteins essential for this mycoplasma gliding was also suggested in the present study.

Dataset Information

Directed Binding of Gliding Bacterium, Mycoplasma mobile, Shown by Detachment Force and Bond Lifetime.

Unlabelled

Importance

Publications

Directed Binding of Gliding Bacterium, Mycoplasma mobile, Shown by Detachment Force and Bond Lifetime.

Similar Datasets

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