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High frequency, spontaneous motA mutations in Campylobacter jejuni strain 81-176.

Mohawk KL, Poly F, Sahl JW, Rasko DA, Guerry P - PLoS ONE (2014)

Bottom Line: However, the only mutated open reading frame common between the two translucent variants and absent from the opaque variants and the parent was motA, encoding a flagellar motor protein.A total of 18 spontaneous motA mutations were found that mapped to four distinct sites in the gene, with only one class of mutation present in a phase variable region.This study exemplifies the mutative/adaptive properties of C. jejuni and demonstrates additional variability in C. jejuni beyond phase variation.

View Article: PubMed Central - PubMed

Affiliation: Enteric Diseases Department, Naval Medical Research Center, Silver Spring, Maryland, United States of America.

ABSTRACT
Campylobacter jejuni is an important cause of bacterial diarrhea worldwide. The pathogenesis of C. jejuni is poorly understood and complicated by phase variation of multiple surface structures including lipooligosaccharide, capsule, and flagellum. When C. jejuni strain 81-176 was plated on blood agar for single colonies, the presence of translucent, non-motile colonial variants was noted among the majority of opaque, motile colonies. High-throughput genomic sequencing of two flagellated translucent and two opaque variants as well as the parent strain revealed multiple genetic changes compared to the published genome. However, the only mutated open reading frame common between the two translucent variants and absent from the opaque variants and the parent was motA, encoding a flagellar motor protein. A total of 18 spontaneous motA mutations were found that mapped to four distinct sites in the gene, with only one class of mutation present in a phase variable region. This study exemplifies the mutative/adaptive properties of C. jejuni and demonstrates additional variability in C. jejuni beyond phase variation.

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Amino acid alignment of MotA.The motA mutations are predicted to result in non-functional proteins. A missense mutation at base 262 (T1, Type B) resulted in an A to P mutation at amino acid 88; a nonsense mutation at base 612 (T3, Type D) resulted in a premature truncation; a duplication of 49 bp created a direct repeat within motA and led to the replacement of the last 73 residues in the C-terminus with a sequence of 39 new residues that are highlighted (T108, Type C); and a deletion at base 64 resulting in a truncated protein (T158, Type A).
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pone-0088043-g004: Amino acid alignment of MotA.The motA mutations are predicted to result in non-functional proteins. A missense mutation at base 262 (T1, Type B) resulted in an A to P mutation at amino acid 88; a nonsense mutation at base 612 (T3, Type D) resulted in a premature truncation; a duplication of 49 bp created a direct repeat within motA and led to the replacement of the last 73 residues in the C-terminus with a sequence of 39 new residues that are highlighted (T108, Type C); and a deletion at base 64 resulting in a truncated protein (T158, Type A).

Mentions: The only mutated open reading frame common to both sequenced T variants but absent from the O variants, 81-176/55, and the two published 81-176 sequences was CJJ81176_0359, encoding the flagellar motor protein MotA. Interestingly, the two sequenced T variants each had distinct mutations in motA. Variant T1 had a G to C transversion at base pair 262 (labeled B in Figure 3) that resulted in an A87P mutation (Figure 4). Variant T3 had a SNP at base 612 that resulted in a G5 to G4 tract change (labeled D in Figure 3) and led to a truncation of 53 amino acid residues in the C-terminus of MotA (Figure 4).


High frequency, spontaneous motA mutations in Campylobacter jejuni strain 81-176.

Mohawk KL, Poly F, Sahl JW, Rasko DA, Guerry P - PLoS ONE (2014)

Amino acid alignment of MotA.The motA mutations are predicted to result in non-functional proteins. A missense mutation at base 262 (T1, Type B) resulted in an A to P mutation at amino acid 88; a nonsense mutation at base 612 (T3, Type D) resulted in a premature truncation; a duplication of 49 bp created a direct repeat within motA and led to the replacement of the last 73 residues in the C-terminus with a sequence of 39 new residues that are highlighted (T108, Type C); and a deletion at base 64 resulting in a truncated protein (T158, Type A).
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3928116&req=5

pone-0088043-g004: Amino acid alignment of MotA.The motA mutations are predicted to result in non-functional proteins. A missense mutation at base 262 (T1, Type B) resulted in an A to P mutation at amino acid 88; a nonsense mutation at base 612 (T3, Type D) resulted in a premature truncation; a duplication of 49 bp created a direct repeat within motA and led to the replacement of the last 73 residues in the C-terminus with a sequence of 39 new residues that are highlighted (T108, Type C); and a deletion at base 64 resulting in a truncated protein (T158, Type A).
Mentions: The only mutated open reading frame common to both sequenced T variants but absent from the O variants, 81-176/55, and the two published 81-176 sequences was CJJ81176_0359, encoding the flagellar motor protein MotA. Interestingly, the two sequenced T variants each had distinct mutations in motA. Variant T1 had a G to C transversion at base pair 262 (labeled B in Figure 3) that resulted in an A87P mutation (Figure 4). Variant T3 had a SNP at base 612 that resulted in a G5 to G4 tract change (labeled D in Figure 3) and led to a truncation of 53 amino acid residues in the C-terminus of MotA (Figure 4).

Bottom Line: However, the only mutated open reading frame common between the two translucent variants and absent from the opaque variants and the parent was motA, encoding a flagellar motor protein.A total of 18 spontaneous motA mutations were found that mapped to four distinct sites in the gene, with only one class of mutation present in a phase variable region.This study exemplifies the mutative/adaptive properties of C. jejuni and demonstrates additional variability in C. jejuni beyond phase variation.

View Article: PubMed Central - PubMed

Affiliation: Enteric Diseases Department, Naval Medical Research Center, Silver Spring, Maryland, United States of America.

ABSTRACT
Campylobacter jejuni is an important cause of bacterial diarrhea worldwide. The pathogenesis of C. jejuni is poorly understood and complicated by phase variation of multiple surface structures including lipooligosaccharide, capsule, and flagellum. When C. jejuni strain 81-176 was plated on blood agar for single colonies, the presence of translucent, non-motile colonial variants was noted among the majority of opaque, motile colonies. High-throughput genomic sequencing of two flagellated translucent and two opaque variants as well as the parent strain revealed multiple genetic changes compared to the published genome. However, the only mutated open reading frame common between the two translucent variants and absent from the opaque variants and the parent was motA, encoding a flagellar motor protein. A total of 18 spontaneous motA mutations were found that mapped to four distinct sites in the gene, with only one class of mutation present in a phase variable region. This study exemplifies the mutative/adaptive properties of C. jejuni and demonstrates additional variability in C. jejuni beyond phase variation.

Show MeSH
Related in: MedlinePlus