A hag mutant of Moraxella catarrhalis strain O35E is deficient in hemagglutination, autoagglutination, and immunoglobulin D-binding activities

Melanie M. Pearson, Eric R. Lafontaine, Nikki J. Wagner, Joseph W. St. Geme, Eric J. Hansen

Research output: Contribution to journalArticle

73 Citations (Scopus)

Abstract

Previous studies correlated the presence of a 200-kDa protein on the surface of Moraxella catarrhalis with the ability of this organism to agglutinate human erythrocytes (M. Fitzgerald, R. Mulcahy, S. Murphy, C. Keane, D. Coakley, and T. Scott, FEMS Immunol. Med. Microbiol. 18:209-216, 1997). In the present study, the gene encoding the 200-kDa protein (designated Hag) of M. catarrhalis strain O35E was subjected to nucleotide sequence analysis and then was inactivated by insertional mutagenesis. The isogenic hag mutant was unable to agglutinate human erythrocytes and lost its ability to autoagglutinate but was still attached at wild-type levels to several human epithelial cell lines. The hag mutation also eliminated the ability of this mutant strain to bind human immunoglobulin D. The presence of the Hag protein on the M. catarrhalis cell surface, as well as that of the UspA1 and UspA2 proteins (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), was investigated by transmission electron and cryoimmunoelectron microscopy. Wild-type M. catarrhalis strain O35E possessed a dense layer of surface projections, whereas an isogenic uspA1 uspA2 hag triple mutant version of this strain did not possess any detectable surface projections. Examination of a uspA1 uspA2 double mutant that expressed the Hag protein revealed the presence of a relatively sparse layer of surface projections, similar to those seen on a uspA2 hag mutant that expressed UspA1. In contrast, a uspA1 hag mutant that expressed UspA2 formed a very dense layer of relatively short surface projections. These results indicate that the surface-exposed Hag protein and UspA1 and UspA2 have the potential to interact both with each other and directly with host defense systems.

Original languageEnglish (US)
Pages (from-to)4523-4533
Number of pages11
JournalInfection and Immunity
Volume70
Issue number8
DOIs
StatePublished - 2002

Fingerprint

Moraxella (Branhamella) catarrhalis
Immunoglobulin D
Hemagglutination
Proteins
Erythrocytes
Insertional Mutagenesis
Protein C
Transmission Electron Microscopy
Sequence Analysis
Membrane Proteins
Epithelial Cells
Cell Line
Mutation
Genes

ASJC Scopus subject areas

  • Immunology

Cite this

A hag mutant of Moraxella catarrhalis strain O35E is deficient in hemagglutination, autoagglutination, and immunoglobulin D-binding activities. / Pearson, Melanie M.; Lafontaine, Eric R.; Wagner, Nikki J.; St. Geme, Joseph W.; Hansen, Eric J.

In: Infection and Immunity, Vol. 70, No. 8, 2002, p. 4523-4533.

Research output: Contribution to journalArticle

Pearson, Melanie M. ; Lafontaine, Eric R. ; Wagner, Nikki J. ; St. Geme, Joseph W. ; Hansen, Eric J. / A hag mutant of Moraxella catarrhalis strain O35E is deficient in hemagglutination, autoagglutination, and immunoglobulin D-binding activities. In: Infection and Immunity. 2002 ; Vol. 70, No. 8. pp. 4523-4533.
@article{b81ee10e4b70478bb16af294f3bec10b,
title = "A hag mutant of Moraxella catarrhalis strain O35E is deficient in hemagglutination, autoagglutination, and immunoglobulin D-binding activities",
abstract = "Previous studies correlated the presence of a 200-kDa protein on the surface of Moraxella catarrhalis with the ability of this organism to agglutinate human erythrocytes (M. Fitzgerald, R. Mulcahy, S. Murphy, C. Keane, D. Coakley, and T. Scott, FEMS Immunol. Med. Microbiol. 18:209-216, 1997). In the present study, the gene encoding the 200-kDa protein (designated Hag) of M. catarrhalis strain O35E was subjected to nucleotide sequence analysis and then was inactivated by insertional mutagenesis. The isogenic hag mutant was unable to agglutinate human erythrocytes and lost its ability to autoagglutinate but was still attached at wild-type levels to several human epithelial cell lines. The hag mutation also eliminated the ability of this mutant strain to bind human immunoglobulin D. The presence of the Hag protein on the M. catarrhalis cell surface, as well as that of the UspA1 and UspA2 proteins (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), was investigated by transmission electron and cryoimmunoelectron microscopy. Wild-type M. catarrhalis strain O35E possessed a dense layer of surface projections, whereas an isogenic uspA1 uspA2 hag triple mutant version of this strain did not possess any detectable surface projections. Examination of a uspA1 uspA2 double mutant that expressed the Hag protein revealed the presence of a relatively sparse layer of surface projections, similar to those seen on a uspA2 hag mutant that expressed UspA1. In contrast, a uspA1 hag mutant that expressed UspA2 formed a very dense layer of relatively short surface projections. These results indicate that the surface-exposed Hag protein and UspA1 and UspA2 have the potential to interact both with each other and directly with host defense systems.",
author = "Pearson, {Melanie M.} and Lafontaine, {Eric R.} and Wagner, {Nikki J.} and {St. Geme}, {Joseph W.} and Hansen, {Eric J.}",
year = "2002",
doi = "10.1128/IAI.70.8.4523-4533.2002",
language = "English (US)",
volume = "70",
pages = "4523--4533",
journal = "Infection and Immunity",
issn = "0019-9567",
publisher = "American Society for Microbiology",
number = "8",

}

TY - JOUR

T1 - A hag mutant of Moraxella catarrhalis strain O35E is deficient in hemagglutination, autoagglutination, and immunoglobulin D-binding activities

AU - Pearson, Melanie M.

AU - Lafontaine, Eric R.

AU - Wagner, Nikki J.

AU - St. Geme, Joseph W.

AU - Hansen, Eric J.

PY - 2002

Y1 - 2002

N2 - Previous studies correlated the presence of a 200-kDa protein on the surface of Moraxella catarrhalis with the ability of this organism to agglutinate human erythrocytes (M. Fitzgerald, R. Mulcahy, S. Murphy, C. Keane, D. Coakley, and T. Scott, FEMS Immunol. Med. Microbiol. 18:209-216, 1997). In the present study, the gene encoding the 200-kDa protein (designated Hag) of M. catarrhalis strain O35E was subjected to nucleotide sequence analysis and then was inactivated by insertional mutagenesis. The isogenic hag mutant was unable to agglutinate human erythrocytes and lost its ability to autoagglutinate but was still attached at wild-type levels to several human epithelial cell lines. The hag mutation also eliminated the ability of this mutant strain to bind human immunoglobulin D. The presence of the Hag protein on the M. catarrhalis cell surface, as well as that of the UspA1 and UspA2 proteins (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), was investigated by transmission electron and cryoimmunoelectron microscopy. Wild-type M. catarrhalis strain O35E possessed a dense layer of surface projections, whereas an isogenic uspA1 uspA2 hag triple mutant version of this strain did not possess any detectable surface projections. Examination of a uspA1 uspA2 double mutant that expressed the Hag protein revealed the presence of a relatively sparse layer of surface projections, similar to those seen on a uspA2 hag mutant that expressed UspA1. In contrast, a uspA1 hag mutant that expressed UspA2 formed a very dense layer of relatively short surface projections. These results indicate that the surface-exposed Hag protein and UspA1 and UspA2 have the potential to interact both with each other and directly with host defense systems.

AB - Previous studies correlated the presence of a 200-kDa protein on the surface of Moraxella catarrhalis with the ability of this organism to agglutinate human erythrocytes (M. Fitzgerald, R. Mulcahy, S. Murphy, C. Keane, D. Coakley, and T. Scott, FEMS Immunol. Med. Microbiol. 18:209-216, 1997). In the present study, the gene encoding the 200-kDa protein (designated Hag) of M. catarrhalis strain O35E was subjected to nucleotide sequence analysis and then was inactivated by insertional mutagenesis. The isogenic hag mutant was unable to agglutinate human erythrocytes and lost its ability to autoagglutinate but was still attached at wild-type levels to several human epithelial cell lines. The hag mutation also eliminated the ability of this mutant strain to bind human immunoglobulin D. The presence of the Hag protein on the M. catarrhalis cell surface, as well as that of the UspA1 and UspA2 proteins (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), was investigated by transmission electron and cryoimmunoelectron microscopy. Wild-type M. catarrhalis strain O35E possessed a dense layer of surface projections, whereas an isogenic uspA1 uspA2 hag triple mutant version of this strain did not possess any detectable surface projections. Examination of a uspA1 uspA2 double mutant that expressed the Hag protein revealed the presence of a relatively sparse layer of surface projections, similar to those seen on a uspA2 hag mutant that expressed UspA1. In contrast, a uspA1 hag mutant that expressed UspA2 formed a very dense layer of relatively short surface projections. These results indicate that the surface-exposed Hag protein and UspA1 and UspA2 have the potential to interact both with each other and directly with host defense systems.

UR - http://www.scopus.com/inward/record.url?scp=0036073628&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036073628&partnerID=8YFLogxK

U2 - 10.1128/IAI.70.8.4523-4533.2002

DO - 10.1128/IAI.70.8.4523-4533.2002

M3 - Article

C2 - 12117964

AN - SCOPUS:0036073628

VL - 70

SP - 4523

EP - 4533

JO - Infection and Immunity

JF - Infection and Immunity

SN - 0019-9567

IS - 8

ER -