scholarly journals Production and characterization of recombinant P1 adhesin essential for adhesion, gliding, and antigenic variation in the human pathogenic bacterium, Mycoplasma pneumoniae

2019 ◽  
Vol 508 (4) ◽  
pp. 1050-1055 ◽  
Author(s):  
Tsuyoshi Kenri ◽  
Yoshito Kawakita ◽  
Hisashi Kudo ◽  
U. Matsumoto ◽  
Shigetarou Mori ◽  
...  
Keyword(s):  
Mycoplasma Pneumoniae ◽  
Antigenic Variation ◽  
Pathogenic Bacterium ◽  
Human Pathogenic Bacterium

scholarly journals Force and Stepwise Movements of Gliding Motility in Human Pathogenic Bacterium Mycoplasma pneumoniae

2021 ◽  
Vol 12 ◽  
Author(s):  
Masaki Mizutani ◽  
Yuya Sasajima ◽  
Makoto Miyata
Keyword(s):  
Optical Tweezers ◽  
Mycoplasma Pneumoniae ◽  
Binding Activity ◽  
Gliding Motility ◽  
Pathogenic Bacterium ◽  
Step Size ◽  
Bacterial Surface ◽  
Human Pathogenic Bacterium ◽  
A Cell ◽  
Stall Force

Mycoplasma pneumoniae, a human pathogenic bacterium, binds to sialylated oligosaccharides and glides on host cell surfaces via a unique mechanism. Gliding motility is essential for initiating the infectious process. In the present study, we measured the stall force of an M. pneumoniae cell carrying a bead that was manipulated using optical tweezers on two strains. The stall forces of M129 and FH strains were averaged to be 23.7 and 19.7 pN, respectively, much weaker than those of other bacterial surface motilities. The binding activity and gliding speed of the M129 strain on sialylated oligosaccharides were eight and two times higher than those of the FH strain, respectively, showing that binding activity is not linked to gliding force. Gliding speed decreased when cell binding was reduced by addition of free sialylated oligosaccharides, indicating the existence of a drag force during gliding. We detected stepwise movements, likely caused by a single leg under 0.2-0.3 mM free sialylated oligosaccharides. A step size of 14-19 nm showed that 25-35 propulsion steps per second are required to achieve the usual gliding speed. The step size was reduced to less than half with the load applied using optical tweezers, showing that a 2.5 pN force from a cell is exerted on a leg. The work performed in this step was 16-30% of the free energy of the hydrolysis of ATP molecules, suggesting that this step is linked to the elementary process of M. pneumoniae gliding. We discuss a model to explain the gliding mechanism, based on the information currently available.

scholarly journals Force and step size of gliding motility in human pathogenic bacterium Mycoplasma pneumoniae

2021 ◽  
Author(s):  
Masaki Mizutani ◽  
Yuya Sasajima ◽  
Makoto Miyata
Keyword(s):  
Optical Tweezers ◽  
Mycoplasma Pneumoniae ◽  
Binding Activity ◽  
Gliding Motility ◽  
Pathogenic Bacterium ◽  
Step Size ◽  
Bacterial Surface ◽  
Human Pathogenic Bacterium ◽  
A Cell ◽  
Stall Force

Mycoplasma pneumoniae, a human pathogenic bacterium, binds to sialylated oligosaccharides and glides on host cell surfaces via a unique mechanism. Gliding motility is essential for initiating the infectious process. In the present study, we measured the stall force of an M. pneumoniae cell carrying a bead that was manipulated using optical tweezers on two strains. The stall forces of M129 and FH strains were averaged to be 23.7 and 19.7 pN, respectively, much weaker than those of other bacterial surface motilities. The binding activity and gliding speed on sialylated oligosaccharides of the M129 strain were eight and two times higher than those of the FH strain, respectively, showing that binding activity is not linked to gliding force. Gliding speed decreased when cell binding was reduced by addition of free sialylated oligosaccharides, indicating the existence of a drag force during gliding. We detected stepwise movements under 0.2‒0.3 mM free sialylated oligosaccharides. A step size of 14‒19 nm showed that 25‒35 propulsion steps per second are required to achieve the usual gliding speed. The step size was reduced to less than half with the load applied using optical tweezers, showing that a 2.5 pN force from a cell is exerted on a leg. The work performed in this step was 16‒30% of the free energy of the hydrolysis of ATP molecules, suggesting that this step is linked to the elementary process of M. pneumoniae gliding.

scholarly journals Characterization of MGC2, a Mycoplasma gallisepticum Cytadhesin with Homology to the Mycoplasma pneumoniae 30-Kilodalton Protein P30 and Mycoplasma genitalium P32

1998 ◽  
Vol 66 (7) ◽  
pp. 3436-3442 ◽  
Author(s):  
Linda L. Hnatow ◽  
Calvin L. Keeler ◽  
Laura L. Tessmer ◽  
Kirk Czymmek ◽  
John E. Dohms
Keyword(s):  
Mycoplasma Pneumoniae ◽  
Reverse Transcription ◽  
Mycoplasma Genitalium ◽  
Mycoplasma Gallisepticum ◽  
Immunogold Labeling ◽  
Respiratory Pathogen ◽  
Functional Studies ◽  
Reverse Transcription Pcr ◽  
Attachment Inhibition

ABSTRACT A second cytadhesin-like protein, MGC2, was identified in the avian respiratory pathogen Mycoplasma gallisepticum. The 912-nucleotide mgc2 gene encodes a 32.6-kDa protein with 40.9 and 31.4% identity with the M. pneumoniae P30 andM. genitalium P32 cytadhesins, respectively. Functional studies with reverse transcription-PCR, immunoblotting, double-sided immunogold labeling, and attachment inhibition assays demonstrated homology to the human mycoplasmal P30 and P32 cytadhesins. These findings suggest that there is a family of cytadhesin genes conserved among pathogenic mycoplasmas infecting widely divergent hosts.

First Detection and Characterization of Macrolide-Resistant Mycoplasma pneumoniae from People with Community-Acquired Pneumonia in Iran

2020 ◽  
Vol 26 (3) ◽  
pp. 245-250 ◽  
Author(s):  
Narjes Noori Goodarzi ◽  
Mohammad Reza Pourmand ◽  
Maryam Arfaatabar ◽  
Ghasem Azimi ◽  
Ensieh Masoorian ◽  
...  
Keyword(s):  
Mycoplasma Pneumoniae ◽  
Community Acquired Pneumonia

scholarly journals Periodicity in Attachment Organelle Revealed by Electron Cryotomography Suggests Conformational Changes in Gliding Mechanism ofMycoplasma pneumoniae

mBio ◽  
2016 ◽  
Vol 7 (2) ◽  
Author(s):  
Akihiro Kawamoto ◽  
Lisa Matsuo ◽  
Takayuki Kato ◽  
Hiroki Yamamoto ◽  
Keiichi Namba ◽  
...  
Keyword(s):  
Mycoplasma Pneumoniae ◽  
Conformational Changes ◽  
Hexagonal Lattice ◽  
Gliding Motility ◽  
Influenza Viruses ◽  
Pathogenic Bacterium ◽  
Dimensional Structure ◽  
Internal Core ◽  
Electron Cryotomography ◽  
Gliding Mechanism

ABSTRACTMycoplasma pneumoniae, a pathogenic bacterium, glides on host surfaces using a unique mechanism. It forms an attachment organelle at a cell pole as a protrusion comprised of knoblike surface structures and an internal core. Here, we analyzed the three-dimensional structure of the organelle in detail by electron cryotomography. On the surface, knoblike particles formed a two-dimensional array, albeit with limited regularity. Analyses using a nonbinding mutant and an antibody showed that the knoblike particles correspond to a naplike structure that has been observed by negative-staining electron microscopy and is likely to be formed as a complex of P1 adhesin, the key protein for binding and gliding. The paired thin and thick plates feature a rigid hexagonal lattice and striations with highly variable repeat distances, respectively. The combination of variable and invariant structures in the internal core and the P1 adhesin array on the surface suggest a model in which axial extension and compression of the thick plate along a rigid thin plate is coupled with attachment to and detachment from the substrate during gliding.IMPORTANCEHuman mycoplasma pneumonia, epidemic all over the world in recent years, is caused by a pathogenic bacterium,Mycoplasma pneumoniae. This tiny bacterium, about 2 µm in cell body length, glides on the surface of the human trachea to infect the host by binding to sialylated oligosaccharides, which are also the binding targets of influenza viruses. The mechanism of mycoplasmal gliding motility is not related to any other well-studied motility systems, such as bacterial flagella and cytoplasmic motor proteins. Here, we visualized the attachment organelle, a cellular architecture for gliding, three dimensionally by using electron cryotomography and other conventional methods. A possible gliding mechanism has been suggested based on the architectural images.

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