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The polar and lateral flagella from Plesiomonas shigelloides are glycosylated with legionaminic acid.

Merino S, Aquilini E, Fulton KM, Twine SM, Tomás JM - Front Microbiol (2015)

Bottom Line: It is the first bacterium reported with O-glycosylated Leg in both polar and lateral flagella.The flagella O-glycosylation is essential for bacterial flagella formation, either polar or lateral, because gene mutants on the biosynthesis of Leg are non-flagellated.Furthermore, the presence of the lateral flagella cluster and Leg O-flagella glycosylation genes are widely spread features among the P. shigelloides strains tested.

View Article: PubMed Central - PubMed

Affiliation: Departamento de Microbiología, Facultad de Biología, Universidad de Barcelona Barcelona, Spain.

ABSTRACT
Plesiomonas shigelloides is the unique member of the Enterobacteriaceae family able to produce polar flagella when grow in liquid medium and lateral flagella when grown in solid or semisolid media. In this study on P. shigelloides 302-73 strain, we found two different gene clusters, one exclusively for the lateral flagella biosynthesis and the other one containing the biosynthetic polar flagella genes with additional putative glycosylation genes. P. shigelloides is the first Enterobacteriaceae were a complete lateral flagella cluster leading to a lateral flagella production is described. We also show that both flagella in P. shigelloides 302-73 strain are glycosylated by a derivative of legionaminic acid (Leg), which explains the presence of Leg pathway genes between the two polar flagella regions in their biosynthetic gene cluster. It is the first bacterium reported with O-glycosylated Leg in both polar and lateral flagella. The flagella O-glycosylation is essential for bacterial flagella formation, either polar or lateral, because gene mutants on the biosynthesis of Leg are non-flagellated. Furthermore, the presence of the lateral flagella cluster and Leg O-flagella glycosylation genes are widely spread features among the P. shigelloides strains tested.

No MeSH data available.


Related in: MedlinePlus

Glycan fragmentation pattern. Front end collision induced dissociation of polar flagellin protein, showing low m/z region. Fragment ions characteristic of an acetylated nonulosonic acid sugar are present.
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Figure 7: Glycan fragmentation pattern. Front end collision induced dissociation of polar flagellin protein, showing low m/z region. Fragment ions characteristic of an acetylated nonulosonic acid sugar are present.

Mentions: Purified polar flagellin preparations showed a well-resolved ion envelop of multiple charged protein ions, which deconvoluted into three distinct masses at 40201, 40652, and 40931 Da. The mass of the translated gene sequence for polar flagellin was 38710 Da, giving mass excesses of 1491, 1942, and 2221 Da, respectively (data not shown). During front end CID experiments of the purified polar flagellin preparation, labile glycan related ions were observed at m/z 359 and 317. Using increasing cone voltages, fragmentation of this ion at m/z 359 was observed, as shown in Figure 7. The fragment ions observed at m/z 317, 299, 281, 222, and 181 were characteristic fragment ions of nonulosonic acids, such as pseudaminic or legionaminic acid.


The polar and lateral flagella from Plesiomonas shigelloides are glycosylated with legionaminic acid.

Merino S, Aquilini E, Fulton KM, Twine SM, Tomás JM - Front Microbiol (2015)

Glycan fragmentation pattern. Front end collision induced dissociation of polar flagellin protein, showing low m/z region. Fragment ions characteristic of an acetylated nonulosonic acid sugar are present.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4481668&req=5

Figure 7: Glycan fragmentation pattern. Front end collision induced dissociation of polar flagellin protein, showing low m/z region. Fragment ions characteristic of an acetylated nonulosonic acid sugar are present.
Mentions: Purified polar flagellin preparations showed a well-resolved ion envelop of multiple charged protein ions, which deconvoluted into three distinct masses at 40201, 40652, and 40931 Da. The mass of the translated gene sequence for polar flagellin was 38710 Da, giving mass excesses of 1491, 1942, and 2221 Da, respectively (data not shown). During front end CID experiments of the purified polar flagellin preparation, labile glycan related ions were observed at m/z 359 and 317. Using increasing cone voltages, fragmentation of this ion at m/z 359 was observed, as shown in Figure 7. The fragment ions observed at m/z 317, 299, 281, 222, and 181 were characteristic fragment ions of nonulosonic acids, such as pseudaminic or legionaminic acid.

Bottom Line: It is the first bacterium reported with O-glycosylated Leg in both polar and lateral flagella.The flagella O-glycosylation is essential for bacterial flagella formation, either polar or lateral, because gene mutants on the biosynthesis of Leg are non-flagellated.Furthermore, the presence of the lateral flagella cluster and Leg O-flagella glycosylation genes are widely spread features among the P. shigelloides strains tested.

View Article: PubMed Central - PubMed

Affiliation: Departamento de Microbiología, Facultad de Biología, Universidad de Barcelona Barcelona, Spain.

ABSTRACT
Plesiomonas shigelloides is the unique member of the Enterobacteriaceae family able to produce polar flagella when grow in liquid medium and lateral flagella when grown in solid or semisolid media. In this study on P. shigelloides 302-73 strain, we found two different gene clusters, one exclusively for the lateral flagella biosynthesis and the other one containing the biosynthetic polar flagella genes with additional putative glycosylation genes. P. shigelloides is the first Enterobacteriaceae were a complete lateral flagella cluster leading to a lateral flagella production is described. We also show that both flagella in P. shigelloides 302-73 strain are glycosylated by a derivative of legionaminic acid (Leg), which explains the presence of Leg pathway genes between the two polar flagella regions in their biosynthetic gene cluster. It is the first bacterium reported with O-glycosylated Leg in both polar and lateral flagella. The flagella O-glycosylation is essential for bacterial flagella formation, either polar or lateral, because gene mutants on the biosynthesis of Leg are non-flagellated. Furthermore, the presence of the lateral flagella cluster and Leg O-flagella glycosylation genes are widely spread features among the P. shigelloides strains tested.

No MeSH data available.


Related in: MedlinePlus