This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hamilton, A. J.
Right arrow Articles by Hay, R. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hamilton, A. J.
Right arrow Articles by Hay, R. J.

 Previous Article  |  Next Article 

Infection and Immunity, December 1998, p. 6024-6026, Vol. 66, No. 12
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Sialic Acid-Dependent Recognition of Laminin by Penicillium marneffei Conidia

A. J. Hamilton,1,2,* L. Jeavons,1,2 S. Youngchim,2 N. Vanittanakom,2 and R. J. Hay1

Dunhill Dermatology Unit, St John's Institute of Dermatology, Guy's Hospital, London, United Kingdom,1 and Microbiology Department, Faculty of Medicine, Chiang Mai University, Chiang Mai, Thailand2

Received 12 June 1998/Returned for modification 21 July 1998/Accepted 25 September 1998

Immunofluorescence microscopy demonstrated that laminin bound to the surface of Penicillium marneffei conidia. Attachment of P. marneffei conidia in an adherence assay was inhibited by soluble laminin and anti-laminin antibody. N-Acetylneuraminic acid abolished adherence, indicating an interaction mediated by a sialic acid-specific lectin.

* Corresponding author. Mailing address: Dunhill Dermatology Unit, St John's Institute of Dermatology, 5th Floor, Thomas Guy House, Guy's Hospital, London SE1 9RT, United Kingdom. Phone: 0171 955 4663. Fax: 0171 407 6689. E-mail: a.hamilton{at}umds.ac.uk.

Infection and Immunity, December 1998, p. 6024-6026, Vol. 66, No. 12
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Tiralongo, J., Wohlschlager, T., Tiralongo, E., Kiefel, M. J. (2009). Inhibition of Aspergillus fumigatus conidia binding to extracellular matrix proteins by sialic acids: a pH effect?. Microbiology 155: 3100-3109 [Abstract] [Full Text]  
  • Vanittanakom, N., Cooper, C. R. Jr., Fisher, M. C., Sirisanthana, T. (2006). Penicillium marneffei Infection and Recent Advances in the Epidemiology and Molecular Biology Aspects. Clin. Microbiol. Rev. 19: 95-110 [Abstract] [Full Text]  
  • Gonzalez, A., Gomez, B. L., Diez, S., Hernandez, O., Restrepo, A., Hamilton, A. J., Cano, L. E. (2005). Purification and Partial Characterization of a Paracoccidioides brasiliensis Protein with Capacity To Bind to Extracellular Matrix Proteins. Infect. Immun. 73: 2486-2495 [Abstract] [Full Text]  
  • Tronchin, G., Esnault, K., Sanchez, M., Larcher, G., Marot-Leblond, A., Bouchara, J.-P. (2002). Purification and Partial Characterization of a 32-Kilodalton Sialic Acid-Specific Lectin from Aspergillus fumigatus. Infect. Immun. 70: 6891-6895 [Abstract] [Full Text]  
  • Wasylnka, J. A., Moore, M. M. (2000). Adhesion of Aspergillus Species to Extracellular Matrix Proteins: Evidence for Involvement of Negatively Charged Carbohydrates on the Conidial Surface. Infect. Immun. 68: 3377-3384 [Abstract] [Full Text]  
  • Hamilton, A. J., Jeavons, L., Youngchim, S., Vanittanakom, N. (1999). Recognition of Fibronectin by Penicillium marneffei Conidia via a Sialic Acid-Dependent Process and Its Relationship to the Interaction Between Conidia and Laminin. Infect. Immun. 67: 5200-5205 [Abstract] [Full Text]  
  • Rongrungruang, Y., Levitz, S. M. (1999). Interactions of Penicillium marneffei with Human Leukocytes In Vitro. Infect. Immun. 67: 4732-4736 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»