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Phase Variation in Helicobacter pylori Lipopolysaccharide
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| Zeitschriftentitel: | Infection and Immunity |
|---|---|
| Personen und Körperschaften: | , , , , , , , , , , , , |
| In: | Infection and Immunity, 66, 1998, 1, S. 70-76 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society for Microbiology
|
| Schlagwörter: |
| author_facet |
Appelmelk, B. J. Shiberu, B. Trinks, C. Tapsi, N. Zheng, P. Y. Verboom, T. Maaskant, J. Hokke, C. H. Schiphorst, W. E. C. M. Blanchard, D. Simoons-Smit, I. M. van den Eijnden, D. H. Vandenbroucke-Grauls, C. M. J. E. Appelmelk, B. J. Shiberu, B. Trinks, C. Tapsi, N. Zheng, P. Y. Verboom, T. Maaskant, J. Hokke, C. H. Schiphorst, W. E. C. M. Blanchard, D. Simoons-Smit, I. M. van den Eijnden, D. H. Vandenbroucke-Grauls, C. M. J. E. |
|---|---|
| author |
Appelmelk, B. J. Shiberu, B. Trinks, C. Tapsi, N. Zheng, P. Y. Verboom, T. Maaskant, J. Hokke, C. H. Schiphorst, W. E. C. M. Blanchard, D. Simoons-Smit, I. M. van den Eijnden, D. H. Vandenbroucke-Grauls, C. M. J. E. |
| spellingShingle |
Appelmelk, B. J. Shiberu, B. Trinks, C. Tapsi, N. Zheng, P. Y. Verboom, T. Maaskant, J. Hokke, C. H. Schiphorst, W. E. C. M. Blanchard, D. Simoons-Smit, I. M. van den Eijnden, D. H. Vandenbroucke-Grauls, C. M. J. E. Infection and Immunity Phase Variation in Helicobacter pylori Lipopolysaccharide Infectious Diseases Immunology Microbiology Parasitology |
| author_sort |
appelmelk, b. j. |
| spelling |
Appelmelk, B. J. Shiberu, B. Trinks, C. Tapsi, N. Zheng, P. Y. Verboom, T. Maaskant, J. Hokke, C. H. Schiphorst, W. E. C. M. Blanchard, D. Simoons-Smit, I. M. van den Eijnden, D. H. Vandenbroucke-Grauls, C. M. J. E. 0019-9567 1098-5522 American Society for Microbiology Infectious Diseases Immunology Microbiology Parasitology http://dx.doi.org/10.1128/iai.66.1.70-76.1998 <jats:title>ABSTRACT</jats:title> <jats:p> <jats:italic>Helicobacter pylori</jats:italic> NCTC 11637 lipopolysaccharide (LPS) expresses the human blood group antigen Lewis x (Le <jats:sup>x</jats:sup> ) in a polymeric form. Le <jats:sup>x</jats:sup> is β- <jats:sc>d</jats:sc> -galactose-(1-4)-[α- <jats:sc>l</jats:sc> -fucose-(1-3)]-β- <jats:sc>d</jats:sc> -acetylglucosamine. Schematically the LPS structure is (Le <jats:sup>x</jats:sup> ) <jats:sub> <jats:italic>n</jats:italic> </jats:sub> -core-lipid A. In this report, we show that Le <jats:sup>x</jats:sup> expression is not a stable trait but that LPS displays a high frequency (0.2 to 0.5%) of phase variation, resulting in the presence of several LPS variants in one bacterial cell population. One type of phase variation implied the loss of α1,3-linked fucose, resulting in variants that expressed nonsubstituted polylactosamines (also called the i antigen), i.e., Le <jats:sup>x</jats:sup> minus fucose; LPS: (lactosamine) <jats:sub> <jats:italic>n</jats:italic> </jats:sub> -core-lipid A. The switch of Le <jats:sup>x</jats:sup> to i antigen was reversible. A second group of variants arose by loss of polymeric main chain which resulted in expression of monomeric Le <jats:sup>y</jats:sup> ; LPS: (Le <jats:sup>y</jats:sup> )-core-lipid A. A third group of variants arose by acquisition of α1,2-linked fucose which hence expressed Le <jats:sup>x</jats:sup> plus Le <jats:sup>y</jats:sup> ; LPS: (Le <jats:sup>y</jats:sup> )(Le <jats:sup>x</jats:sup> ) <jats:sub> <jats:italic>n</jats:italic> </jats:sub> -core-lipid A. The second and third group of variants switched back to the parental phenotype [(Le <jats:sup>x</jats:sup> ) <jats:sub> <jats:italic>n</jats:italic> </jats:sub> -core-lipid A] in lower frequencies. Part of the variation can be ascribed to altered expression levels of glycosyltransferase levels as assessed by assaying the activities of galactosyl-, fucosyl-, and <jats:italic>N</jats:italic> -acetylglucosaminyltransferases. Clearly phase variation increases the heterogeneity of <jats:italic>H. pylori</jats:italic> , and this process may be involved in generating the very closely related yet genetically slightly different strains that have been isolated from one patient. </jats:p> Phase Variation in <i>Helicobacter pylori</i> Lipopolysaccharide Infection and Immunity |
| doi_str_mv |
10.1128/iai.66.1.70-76.1998 |
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Medizin Biologie |
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American Society for Microbiology, 1998 |
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American Society for Microbiology, 1998 |
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0019-9567 1098-5522 |
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0019-9567 1098-5522 |
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appelmelk1998phasevariationinhelicobacterpylorilipopolysaccharide |
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1998 |
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American Society for Microbiology |
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ai |
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ai |
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Infection and Immunity |
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49 |
| title |
Phase Variation in Helicobacter pylori Lipopolysaccharide |
| title_unstemmed |
Phase Variation in Helicobacter pylori Lipopolysaccharide |
| title_full |
Phase Variation in Helicobacter pylori Lipopolysaccharide |
| title_fullStr |
Phase Variation in Helicobacter pylori Lipopolysaccharide |
| title_full_unstemmed |
Phase Variation in Helicobacter pylori Lipopolysaccharide |
| title_short |
Phase Variation in Helicobacter pylori Lipopolysaccharide |
| title_sort |
phase variation in
<i>helicobacter pylori</i>
lipopolysaccharide |
| topic |
Infectious Diseases Immunology Microbiology Parasitology |
| url |
http://dx.doi.org/10.1128/iai.66.1.70-76.1998 |
| publishDate |
1998 |
| physical |
70-76 |
| description |
<jats:title>ABSTRACT</jats:title>
<jats:p>
<jats:italic>Helicobacter pylori</jats:italic>
NCTC 11637 lipopolysaccharide (LPS) expresses the human blood group antigen Lewis x (Le
<jats:sup>x</jats:sup>
) in a polymeric form. Le
<jats:sup>x</jats:sup>
is β-
<jats:sc>d</jats:sc>
-galactose-(1-4)-[α-
<jats:sc>l</jats:sc>
-fucose-(1-3)]-β-
<jats:sc>d</jats:sc>
-acetylglucosamine. Schematically the LPS structure is (Le
<jats:sup>x</jats:sup>
)
<jats:sub>
<jats:italic>n</jats:italic>
</jats:sub>
-core-lipid A. In this report, we show that Le
<jats:sup>x</jats:sup>
expression is not a stable trait but that LPS displays a high frequency (0.2 to 0.5%) of phase variation, resulting in the presence of several LPS variants in one bacterial cell population. One type of phase variation implied the loss of α1,3-linked fucose, resulting in variants that expressed nonsubstituted polylactosamines (also called the i antigen), i.e., Le
<jats:sup>x</jats:sup>
minus fucose; LPS: (lactosamine)
<jats:sub>
<jats:italic>n</jats:italic>
</jats:sub>
-core-lipid A. The switch of Le
<jats:sup>x</jats:sup>
to i antigen was reversible. A second group of variants arose by loss of polymeric main chain which resulted in expression of monomeric Le
<jats:sup>y</jats:sup>
; LPS: (Le
<jats:sup>y</jats:sup>
)-core-lipid A. A third group of variants arose by acquisition of α1,2-linked fucose which hence expressed Le
<jats:sup>x</jats:sup>
plus Le
<jats:sup>y</jats:sup>
; LPS: (Le
<jats:sup>y</jats:sup>
)(Le
<jats:sup>x</jats:sup>
)
<jats:sub>
<jats:italic>n</jats:italic>
</jats:sub>
-core-lipid A. The second and third group of variants switched back to the parental phenotype [(Le
<jats:sup>x</jats:sup>
)
<jats:sub>
<jats:italic>n</jats:italic>
</jats:sub>
-core-lipid A] in lower frequencies. Part of the variation can be ascribed to altered expression levels of glycosyltransferase levels as assessed by assaying the activities of galactosyl-, fucosyl-, and
<jats:italic>N</jats:italic>
-acetylglucosaminyltransferases. Clearly phase variation increases the heterogeneity of
<jats:italic>H. pylori</jats:italic>
, and this process may be involved in generating the very closely related yet genetically slightly different strains that have been isolated from one patient.
</jats:p> |
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| author | Appelmelk, B. J., Shiberu, B., Trinks, C., Tapsi, N., Zheng, P. Y., Verboom, T., Maaskant, J., Hokke, C. H., Schiphorst, W. E. C. M., Blanchard, D., Simoons-Smit, I. M., van den Eijnden, D. H., Vandenbroucke-Grauls, C. M. J. E. |
| author_facet | Appelmelk, B. J., Shiberu, B., Trinks, C., Tapsi, N., Zheng, P. Y., Verboom, T., Maaskant, J., Hokke, C. H., Schiphorst, W. E. C. M., Blanchard, D., Simoons-Smit, I. M., van den Eijnden, D. H., Vandenbroucke-Grauls, C. M. J. E., Appelmelk, B. J., Shiberu, B., Trinks, C., Tapsi, N., Zheng, P. Y., Verboom, T., Maaskant, J., Hokke, C. H., Schiphorst, W. E. C. M., Blanchard, D., Simoons-Smit, I. M., van den Eijnden, D. H., Vandenbroucke-Grauls, C. M. J. E. |
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| description | <jats:title>ABSTRACT</jats:title> <jats:p> <jats:italic>Helicobacter pylori</jats:italic> NCTC 11637 lipopolysaccharide (LPS) expresses the human blood group antigen Lewis x (Le <jats:sup>x</jats:sup> ) in a polymeric form. Le <jats:sup>x</jats:sup> is β- <jats:sc>d</jats:sc> -galactose-(1-4)-[α- <jats:sc>l</jats:sc> -fucose-(1-3)]-β- <jats:sc>d</jats:sc> -acetylglucosamine. Schematically the LPS structure is (Le <jats:sup>x</jats:sup> ) <jats:sub> <jats:italic>n</jats:italic> </jats:sub> -core-lipid A. In this report, we show that Le <jats:sup>x</jats:sup> expression is not a stable trait but that LPS displays a high frequency (0.2 to 0.5%) of phase variation, resulting in the presence of several LPS variants in one bacterial cell population. One type of phase variation implied the loss of α1,3-linked fucose, resulting in variants that expressed nonsubstituted polylactosamines (also called the i antigen), i.e., Le <jats:sup>x</jats:sup> minus fucose; LPS: (lactosamine) <jats:sub> <jats:italic>n</jats:italic> </jats:sub> -core-lipid A. The switch of Le <jats:sup>x</jats:sup> to i antigen was reversible. A second group of variants arose by loss of polymeric main chain which resulted in expression of monomeric Le <jats:sup>y</jats:sup> ; LPS: (Le <jats:sup>y</jats:sup> )-core-lipid A. A third group of variants arose by acquisition of α1,2-linked fucose which hence expressed Le <jats:sup>x</jats:sup> plus Le <jats:sup>y</jats:sup> ; LPS: (Le <jats:sup>y</jats:sup> )(Le <jats:sup>x</jats:sup> ) <jats:sub> <jats:italic>n</jats:italic> </jats:sub> -core-lipid A. The second and third group of variants switched back to the parental phenotype [(Le <jats:sup>x</jats:sup> ) <jats:sub> <jats:italic>n</jats:italic> </jats:sub> -core-lipid A] in lower frequencies. Part of the variation can be ascribed to altered expression levels of glycosyltransferase levels as assessed by assaying the activities of galactosyl-, fucosyl-, and <jats:italic>N</jats:italic> -acetylglucosaminyltransferases. Clearly phase variation increases the heterogeneity of <jats:italic>H. pylori</jats:italic> , and this process may be involved in generating the very closely related yet genetically slightly different strains that have been isolated from one patient. </jats:p> |
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| imprint | American Society for Microbiology, 1998 |
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| spelling | Appelmelk, B. J. Shiberu, B. Trinks, C. Tapsi, N. Zheng, P. Y. Verboom, T. Maaskant, J. Hokke, C. H. Schiphorst, W. E. C. M. Blanchard, D. Simoons-Smit, I. M. van den Eijnden, D. H. Vandenbroucke-Grauls, C. M. J. E. 0019-9567 1098-5522 American Society for Microbiology Infectious Diseases Immunology Microbiology Parasitology http://dx.doi.org/10.1128/iai.66.1.70-76.1998 <jats:title>ABSTRACT</jats:title> <jats:p> <jats:italic>Helicobacter pylori</jats:italic> NCTC 11637 lipopolysaccharide (LPS) expresses the human blood group antigen Lewis x (Le <jats:sup>x</jats:sup> ) in a polymeric form. Le <jats:sup>x</jats:sup> is β- <jats:sc>d</jats:sc> -galactose-(1-4)-[α- <jats:sc>l</jats:sc> -fucose-(1-3)]-β- <jats:sc>d</jats:sc> -acetylglucosamine. Schematically the LPS structure is (Le <jats:sup>x</jats:sup> ) <jats:sub> <jats:italic>n</jats:italic> </jats:sub> -core-lipid A. In this report, we show that Le <jats:sup>x</jats:sup> expression is not a stable trait but that LPS displays a high frequency (0.2 to 0.5%) of phase variation, resulting in the presence of several LPS variants in one bacterial cell population. One type of phase variation implied the loss of α1,3-linked fucose, resulting in variants that expressed nonsubstituted polylactosamines (also called the i antigen), i.e., Le <jats:sup>x</jats:sup> minus fucose; LPS: (lactosamine) <jats:sub> <jats:italic>n</jats:italic> </jats:sub> -core-lipid A. The switch of Le <jats:sup>x</jats:sup> to i antigen was reversible. A second group of variants arose by loss of polymeric main chain which resulted in expression of monomeric Le <jats:sup>y</jats:sup> ; LPS: (Le <jats:sup>y</jats:sup> )-core-lipid A. A third group of variants arose by acquisition of α1,2-linked fucose which hence expressed Le <jats:sup>x</jats:sup> plus Le <jats:sup>y</jats:sup> ; LPS: (Le <jats:sup>y</jats:sup> )(Le <jats:sup>x</jats:sup> ) <jats:sub> <jats:italic>n</jats:italic> </jats:sub> -core-lipid A. The second and third group of variants switched back to the parental phenotype [(Le <jats:sup>x</jats:sup> ) <jats:sub> <jats:italic>n</jats:italic> </jats:sub> -core-lipid A] in lower frequencies. Part of the variation can be ascribed to altered expression levels of glycosyltransferase levels as assessed by assaying the activities of galactosyl-, fucosyl-, and <jats:italic>N</jats:italic> -acetylglucosaminyltransferases. Clearly phase variation increases the heterogeneity of <jats:italic>H. pylori</jats:italic> , and this process may be involved in generating the very closely related yet genetically slightly different strains that have been isolated from one patient. </jats:p> Phase Variation in <i>Helicobacter pylori</i> Lipopolysaccharide Infection and Immunity |
| spellingShingle | Appelmelk, B. J., Shiberu, B., Trinks, C., Tapsi, N., Zheng, P. Y., Verboom, T., Maaskant, J., Hokke, C. H., Schiphorst, W. E. C. M., Blanchard, D., Simoons-Smit, I. M., van den Eijnden, D. H., Vandenbroucke-Grauls, C. M. J. E., Infection and Immunity, Phase Variation in Helicobacter pylori Lipopolysaccharide, Infectious Diseases, Immunology, Microbiology, Parasitology |
| title | Phase Variation in Helicobacter pylori Lipopolysaccharide |
| title_full | Phase Variation in Helicobacter pylori Lipopolysaccharide |
| title_fullStr | Phase Variation in Helicobacter pylori Lipopolysaccharide |
| title_full_unstemmed | Phase Variation in Helicobacter pylori Lipopolysaccharide |
| title_short | Phase Variation in Helicobacter pylori Lipopolysaccharide |
| title_sort | phase variation in <i>helicobacter pylori</i> lipopolysaccharide |
| title_unstemmed | Phase Variation in Helicobacter pylori Lipopolysaccharide |
| topic | Infectious Diseases, Immunology, Microbiology, Parasitology |
| url | http://dx.doi.org/10.1128/iai.66.1.70-76.1998 |