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Volume 18, Number 3—March 2012
Research

Lineage-specific Virulence Determinants of Haemophilus influenzae Biogroup aegyptius

Fiona R. Strouts1, Peter Power, Nicholas J. Croucher, Nicola Corton, Andries van Tonder, Michael A. Quail, Paul R. Langford, Michael J. Hudson, Julian Parkhill, J. Simon KrollComments to Author , and Stephen D. Bentley
Author affiliations: Imperial College London, London, UK (F.R. Strouts, P.R. Langford, J.S. Kroll); University of Oxford, Oxford, UK (P. Power); Wellcome Trust Sanger Institute, Cambridge, UK (N.J. Croucher, N. Corton, A. van Tonder, M.A. Quail, J. Parkhill, S.D. Bentley); The Health Protection Agency, Salisbury, UK (M.J. Hudson)

Main Article

Figure 6

Domain organization of the Haemophilus influenzae biogroup aegyptius trimeric autotransporter adhesins TabA1/TahA1 and TabA2/TahA2, showing differences in passenger domain sequence motifs. Purple, C-terminal translocator domain; red, hemagglutinin domains; green, Hap_Hag domains; orange, degenerate repeats; blue, N terminal signal peptide.

Figure 6. Domain organization of the Haemophilus influenzae biogroup aegyptius trimeric autotransporter adhesins TabA1/TahA1 and TabA2/TahA2, showing differences in passenger domain sequence motifs. Purple, C-terminal translocator domain; red, hemagglutinin domains; green, Hap_Hag domains; orange, degenerate repeats; blue, N terminal signal peptide.

Main Article

1Current affiliation: Stanford University, Palo Alto, California, USA.

Page created: February 16, 2012
Page updated: February 16, 2012
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The conclusions, findings, and opinions expressed by authors contributing to this journal do not necessarily reflect the official position of the U.S. Department of Health and Human Services, the Public Health Service, the Centers for Disease Control and Prevention, or the authors' affiliated institutions. Use of trade names is for identification only and does not imply endorsement by any of the groups named above.
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