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A tick gut protein with fibronectin III domains aids Borrelia burgdorferi congregation to the gut during transmission.

Narasimhan S, Coumou J, Schuijt TJ, Boder E, Hovius JW, Fikrig E - PLoS Pathog. (2014)

Bottom Line: Immunization against Ixofin3D and RNA interference-mediated reduction in expression of Ixofin3D resulted in decreased spirochete burden in tick salivary glands and in the murine host.Microscopic examination showed decreased aggregation of spirochetes on the gut epithelium concomitant with reduced expression of Ixofin3D.Our observations suggest that the interaction between Borrelia and Ixofin3D facilitates spirochete congregation to the gut during transmission, and provides a "molecular exit" direction for spirochete egress from the gut.

View Article: PubMed Central - PubMed

Affiliation: Department of Internal Medicine, Yale University School of Medicine, New Haven, Connecticut, United States of America.

ABSTRACT
Borrelia burgdorferi transmission to the vertebrate host commences with growth of the spirochete in the tick gut and migration from the gut to the salivary glands. This complex process, involving intimate interactions of the spirochete with the gut epithelium, is pivotal to transmission. We utilized a yeast surface display library of tick gut proteins to perform a global screen for tick gut proteins that might interact with Borrelia membrane proteins. A putative fibronectin type III domain-containing tick gut protein (Ixofin3D) was most frequently identified from this screen and prioritized for further analysis. Immunization against Ixofin3D and RNA interference-mediated reduction in expression of Ixofin3D resulted in decreased spirochete burden in tick salivary glands and in the murine host. Microscopic examination showed decreased aggregation of spirochetes on the gut epithelium concomitant with reduced expression of Ixofin3D. Our observations suggest that the interaction between Borrelia and Ixofin3D facilitates spirochete congregation to the gut during transmission, and provides a "molecular exit" direction for spirochete egress from the gut.

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Full-length sequence of Ixofin3D (Genbank accession number KF709698).A. Amino acid (AA) sequence corresponding to: the annotated ISCW008121 (green), fragment obtained by 5′ RNA Ligase Mediated Rapid Amplification of cDNA Ends (RLM-RACE) (grey), yeast surface display Clone 1 (red), fragment obtained by 3′ RLM-RACE (blue), and the annotated ISCW005809 (yellow). B. Predicted analysis of full-length Ixofin3D using the Simple Modular Architecture Research Tool available at http://smart.embl-heidelberg.de.
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ppat-1004278-g002: Full-length sequence of Ixofin3D (Genbank accession number KF709698).A. Amino acid (AA) sequence corresponding to: the annotated ISCW008121 (green), fragment obtained by 5′ RNA Ligase Mediated Rapid Amplification of cDNA Ends (RLM-RACE) (grey), yeast surface display Clone 1 (red), fragment obtained by 3′ RLM-RACE (blue), and the annotated ISCW005809 (yellow). B. Predicted analysis of full-length Ixofin3D using the Simple Modular Architecture Research Tool available at http://smart.embl-heidelberg.de.

Mentions: *Based on Ixofin3D sequence, see Figure 2. ORF: Open Reading Frame.


A tick gut protein with fibronectin III domains aids Borrelia burgdorferi congregation to the gut during transmission.

Narasimhan S, Coumou J, Schuijt TJ, Boder E, Hovius JW, Fikrig E - PLoS Pathog. (2014)

Full-length sequence of Ixofin3D (Genbank accession number KF709698).A. Amino acid (AA) sequence corresponding to: the annotated ISCW008121 (green), fragment obtained by 5′ RNA Ligase Mediated Rapid Amplification of cDNA Ends (RLM-RACE) (grey), yeast surface display Clone 1 (red), fragment obtained by 3′ RLM-RACE (blue), and the annotated ISCW005809 (yellow). B. Predicted analysis of full-length Ixofin3D using the Simple Modular Architecture Research Tool available at http://smart.embl-heidelberg.de.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4125277&req=5

ppat-1004278-g002: Full-length sequence of Ixofin3D (Genbank accession number KF709698).A. Amino acid (AA) sequence corresponding to: the annotated ISCW008121 (green), fragment obtained by 5′ RNA Ligase Mediated Rapid Amplification of cDNA Ends (RLM-RACE) (grey), yeast surface display Clone 1 (red), fragment obtained by 3′ RLM-RACE (blue), and the annotated ISCW005809 (yellow). B. Predicted analysis of full-length Ixofin3D using the Simple Modular Architecture Research Tool available at http://smart.embl-heidelberg.de.
Mentions: *Based on Ixofin3D sequence, see Figure 2. ORF: Open Reading Frame.

Bottom Line: Immunization against Ixofin3D and RNA interference-mediated reduction in expression of Ixofin3D resulted in decreased spirochete burden in tick salivary glands and in the murine host.Microscopic examination showed decreased aggregation of spirochetes on the gut epithelium concomitant with reduced expression of Ixofin3D.Our observations suggest that the interaction between Borrelia and Ixofin3D facilitates spirochete congregation to the gut during transmission, and provides a "molecular exit" direction for spirochete egress from the gut.

View Article: PubMed Central - PubMed

Affiliation: Department of Internal Medicine, Yale University School of Medicine, New Haven, Connecticut, United States of America.

ABSTRACT
Borrelia burgdorferi transmission to the vertebrate host commences with growth of the spirochete in the tick gut and migration from the gut to the salivary glands. This complex process, involving intimate interactions of the spirochete with the gut epithelium, is pivotal to transmission. We utilized a yeast surface display library of tick gut proteins to perform a global screen for tick gut proteins that might interact with Borrelia membrane proteins. A putative fibronectin type III domain-containing tick gut protein (Ixofin3D) was most frequently identified from this screen and prioritized for further analysis. Immunization against Ixofin3D and RNA interference-mediated reduction in expression of Ixofin3D resulted in decreased spirochete burden in tick salivary glands and in the murine host. Microscopic examination showed decreased aggregation of spirochetes on the gut epithelium concomitant with reduced expression of Ixofin3D. Our observations suggest that the interaction between Borrelia and Ixofin3D facilitates spirochete congregation to the gut during transmission, and provides a "molecular exit" direction for spirochete egress from the gut.

Show MeSH
Related in: MedlinePlus