Detailed Analyses of Stall Force Generation in Mycoplasma mobile Gliding

Mizutani, Masaki; Tulum, Isil; Kinosita, Yoshiaki; Nishizaka, Takayuki; Miyata, Makoto

doi:10.1016/j.bpj.2018.01.029

Cited by 24 publications

(66 citation statements)

References 62 publications

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“…Proline at 476 th and serine at 859 th positions in Gli521 are totally diverse but proline at 1461 st position is totally conserved among the four species. Serine at 2770 th position in Gli349 is totally conserved, consistent with the fact that m23 mutant which has this serine mutated to leucine is incapable of binding 23,27 . Using genome sequences of two new species, we evaluated the conservativity of each position.…”

Section: Genome and Sequence Analyses Of The New Gliding Species Thesupporting

confidence: 67%

“…The long flexible part (LFP) comprising the repeat sequences J through V (1248-2720 aa) showed 80 T-Coffee score. The binding positions of the previously described two inhibitory antibodies mAb3 and mAb7, and two mutation points inhibiting binding and gliding were found on Gli349 in m13 and m23 strains 23,27 . These constituted the highly conservative regions corresponding to J-K-L (1248-1546 aa) repeats in the LFP.…”

Section: Genome and Sequence Analyses Of The New Gliding Species Thementioning

confidence: 81%

“…The EYFP fusions caused a reduction in cell binding for MMOB1620 and acceleration in gliding speed for MMOB1640. These results can be explained if we consider the working model explaining the gliding mechanism, where a cycle consists of four steps of interaction including catch, pull, drag and release 5,6,8,27,31 with the binding target, i.e. sialylated oligosaccharides (SOs) [32][33][34] .…”

Section: Discussionmentioning

confidence: 99%

“…Mycoplasma gliding was observed by phase-contrast microscopy using a BX50 microscope (Olympus) and recorded with a Wat-120N CCD camera (Watec, Yamagata, Japan). All video data were analysed by using ImageJ software, version 1.52a (http://rsb.info.nih.gov/ij/), as previously described 27,31,33,37 .…”

Section: Methodsmentioning

confidence: 99%

“…Previously, our group has identified mutations and epitopes in the monoclonal antibody against Gli521 which influenced binding activity and gliding speed. Interestingly, these sequences were never mapped onto the highly conserved regions 23,27 . We then focused on analysing the conservativity of individual mutation points to understand its effect on the function of the protein.…”

Section: Genome and Sequence Analyses Of The New Gliding Species Thementioning

confidence: 99%

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Identification and sequence analyses of the gliding machinery proteins from Mycoplasma mobile

Tulum

Kimura

Miyata

2020

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Mycoplasma mobile, a fish pathogen, exhibits its own specialized gliding motility on host cells based on ATP hydrolysis. The special protein machinery enabling this motility is composed of surface and internal protein complexes. Four proteins, MMOBs 1630, 1660, 1670, and 4860 constitute the internal complex, including paralogs of F-type ATPase/synthase α and β subunits. In the present study, the cellular localisation for the candidate gliding machinery proteins, MMOBs 1620, 1640, 1650, and 5430 was investigated by using a total internal reflection fluorescence microscopy system after tagging these proteins with the enhanced yellow fluorescent protein (EYFP). The M. mobile strain expressing a fusion protein MMOB1620-EYFP exhibited reduced cell-binding activity and a strain expressing MMOB1640 fused with EYFP exhibited increased gliding speed, showing the involvement of these proteins in the gliding mechanism. Based on the genomic sequences, we analysed the sequence conservativity in the proteins of the internal and the surface complexes from four gliding mycoplasma species. The proteins in the internal complex were more conserved compared to the surface complex, suggesting that the surface complex undergoes modifications depending on the host. The analyses suggested that the internal gliding complex was highly conserved probably due to its role in the motility mechanism. Class Mollicutes is mainly represented by Mycoplasma species which are parasitic or occasionally commensal bacteria that have small cell size, small genomes, and no peptidoglycan layer 1,2. More than ten Mycoplasma species show gliding motility. Interestingly, mycoplasma gliding was not connected to flagella, pili, or other bacterial motility systems. This might be due to the loss of the peptidoglycan layer during mycoplasma evolution, because the conventional bacterial motility systems need to be anchored to the peptidoglycan layer 3. Moreover, the motility combined with the ability to adhere to the host cell surface play a key role in its pathogenesis 4. Mycoplasma mobile, a fast-gliding mycoplasma was isolated from the gills of freshwater fish (Fig. 1). It exhibits gliding motility with an average speed of 2.0 to 4.5 μm/s 5-7. M. mobile gliding machinery can be divided into two parts, internal and surface structures 5,8. The surface structure is composed of three huge proteins, Gli123, Gli349, and Gli521 (123, 349, and 521 kDa molecular weights, respectively). Gli42 (42 kDa) should be translated together with the surface proteins but the localisation on the surface has not been clarified. These proteins are involved in the gliding machinery (Fig. 2A) 9-13. Previous studies identified,

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Section: Genome and Sequence Analyses Of The New Gliding Species Thesupporting

confidence: 67%

Section: Genome and Sequence Analyses Of The New Gliding Species Thementioning

confidence: 81%