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MOLECULAR AND CELLULAR PATHOGENESIS

Phenotypic Effect of Isogenic uspA1 anduspA2 Mutations on Moraxella catarrhalis 035E

Christoph Aebi, Eric R. Lafontaine, Leslie D. Cope, Jo L. Latimer, Sheryl L. Lumbley, George H. McCracken Jr., Eric J. Hansen
Christoph Aebi
Departments of Microbiology and
Pediatrics, University of Texas Southwestern Medical Center, Dallas, Texas 75235-9048
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Eric R. Lafontaine
Departments of Microbiology and
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Leslie D. Cope
Departments of Microbiology and
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Jo L. Latimer
Departments of Microbiology and
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Sheryl L. Lumbley
Departments of Microbiology and
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George H. McCracken Jr.
Pediatrics, University of Texas Southwestern Medical Center, Dallas, Texas 75235-9048
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Eric J. Hansen
Departments of Microbiology and
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DOI: 10.1128/IAI.66.7.3113-3119.1998
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ABSTRACT

The UspA surface antigen of Moraxella catarrhalis was recently shown to be comprised of two different proteins (UspA1 and UspA2) which share an internal region containing 140 amino acids with 93% identity (C. Aebi, I. Maciver, J. L. Latimer, L. D. Cope, M. K. Stevens, S. E. Thomas, G. H. McCracken, Jr., and E. J. Hansen, Infect. Immun. 65:4367–4377, 1997). Isogenic uspA1, uspA2, and uspA1 uspA2 mutants were tested in a number of in vitro systems to determine what effect these mutations, either individually or together, might exert on the phenotype of M. catarrhalis 035E. Monoclonal antibodies specific for UspA1 or UspA2 were used in an indirect antibody accessibility assay to prove that both of these proteins were expressed on the surface of M. catarrhalis. All three mutants grew in vitro at the same rate and did not exhibit autoagglutination or hemagglutination properties that were detectably different from those of the wild-type parent strain. When tested for the ability to adhere to human epithelial cells, the wild-type parent strain and the uspA2 mutant readily attached to Chang conjunctival cells. In contrast, theuspA1 mutant and the uspA1 uspA2 double mutant both attached to these epithelial cells at a level nearly 2 orders of magnitude lower than that obtained with the wild-type parent strain, a result which suggested that expression of UspA1 byM. catarrhalis is essential for attachment to these epithelial cells. Both the wild-type parent strain and theuspA1 mutant were resistant to the bactericidal activity of normal human serum, whereas the uspA2 mutant and theuspA1 uspA2 double mutant were readily killed by this serum. This latter result indicated that the presence of UspA2 is essential for expression of serum resistance by M. catarrhalis.

  • Copyright © 1998 American Society for Microbiology
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Phenotypic Effect of Isogenic uspA1 anduspA2 Mutations on Moraxella catarrhalis 035E
Christoph Aebi, Eric R. Lafontaine, Leslie D. Cope, Jo L. Latimer, Sheryl L. Lumbley, George H. McCracken Jr., Eric J. Hansen
Infection and Immunity Jul 1998, 66 (7) 3113-3119; DOI: 10.1128/IAI.66.7.3113-3119.1998

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Phenotypic Effect of Isogenic uspA1 anduspA2 Mutations on Moraxella catarrhalis 035E
Christoph Aebi, Eric R. Lafontaine, Leslie D. Cope, Jo L. Latimer, Sheryl L. Lumbley, George H. McCracken Jr., Eric J. Hansen
Infection and Immunity Jul 1998, 66 (7) 3113-3119; DOI: 10.1128/IAI.66.7.3113-3119.1998
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KEYWORDS

Antigens, Bacterial
Bacterial Outer Membrane Proteins
Moraxella (Branhamella) catarrhalis

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