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Updated: Apr 22, 2026

Adherence of Bacteria to Plant Surfaces Measured in the Laboratory
Published on: June 19, 2018
Onion yellow phytoplasma P38 protein plays a role in adhesion to the hosts
Yutaro Neriya1, Kensaku Maejima, Takamichi Nijo
1Laboratory of Plant Pathology, Department of Agricultural and Environmental Biology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
Abstract:
Adhesins are microbial surface proteins that mediate the adherence of microbial pathogens to host cell surfaces. In Mollicutes, several adhesins have been reported in mycoplasmas and spiroplasmas. Adhesins P40 of Mycoplasma agalactiae and P89 of Spiroplasma citri contain a conserved amino acid sequence known as the Mollicutes adhesin motif (MAM), whose function in the host cell adhesion remains unclear. Here, we show that phytoplasmas, which are plant-pathogenic mollicutes transmitted by insect vectors, possess an adhesion-containing MAM that was identified in a putative membrane protein, PAM289 (P38), of the 'Candidatus Phytoplasma asteris,' OY strain. P38 homologs and their MAMs were highly conserved in related phytoplasma strains. While P38 protein was expressed in OY-infected insect and plant hosts, binding assays showed that P38 interacts with insect extract, and weakly with plant extract. Interestingly, the interaction of P38 with the insect extract depended on MAM. These results suggest that P38 is a phytoplasma adhesin that interacts with the hosts. In addition, the MAM of adhesins is important for the interaction between P38 protein and hosts.
Insights
Phytoplasmas possess a novel adhesin, P38, containing the Mollicutes adhesin motif (MAM). This protein interacts with insect and plant hosts, highlighting MAM's role in phytoplasma adhesion.
Area of Science:
- Microbiology
- Molecular Biology
- Plant Pathology
Background:
- Adhesins mediate microbial pathogen adherence to host cells.
- Mollicutes, including mycoplasmas and spiroplasmas, have known adhesins.
- The Mollicutes adhesin motif (MAM) is conserved but its function is unclear.
Purpose of the Study:
- To identify and characterize adhesins in phytoplasmas.
- To investigate the role of the MAM in phytoplasma-host interactions.
- To determine if P38 is a phytoplasma adhesin.
Main Methods:
- Bioinformatic analysis to identify MAM-containing proteins.
- Expression analysis of P38 in infected hosts.
- In vitro binding assays using insect and plant extracts.
Main Results:
- A putative adhesin, P38, containing MAM was identified in 'Candidatus Phytoplasma asteris' OY strain.
- P38 homologs and MAMs are conserved across phytoplasma strains.
- P38 interacts with insect extracts, dependent on MAM, and weakly with plant extracts.
Conclusions:
- P38 functions as a phytoplasma adhesin mediating host interactions.
- The MAM is crucial for P38's interaction with insect and plant hosts.
- This study elucidates a key mechanism in phytoplasma-vector and phytoplasma-plant adhesion.
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