Isolation and Characterization of Two Proteins fromMoraxella catarrhalis That Bear a Common Epitope

McMichael, John; Fiske, Michael J.; Fredenburg, Ross A.; Chakravarti, Deb N.; VanDerMeid, Karl R.; Barniak, Vicki; Caplan, Jeffrey; Bortell, Eric; Baker, Stephen; Arumugham, Rasappa; Chen, Dexiang

doi:10.1128/.66.9.4374-4381.1998

Cited by 14 publications

(27 citation statements)

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“…When heated lysates were used, a lower molecular weight protein of ≈ 92 kDa became progressively apparent with prolonged heating, which also bound to the receptor. Prolonged heating has been reported to convert UspA1 oligomers of ≈ 250 kDa to monomers that migrate with a reduced apparent M r of ≈ 90–120 kDa (McMichael et al ., 1998). Thus, the migration of the CEACAM‐binding protein on gels was indicative of UspA1 of Mx (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Two UspA genes ( uspA1 and uspA2 ) encoding structurally related but functionally distinct proteins have been described. The UspA proteins bind to extracellular matrix proteins and/or human epithelial cells in vitro (Aebi et al ., 1997; 1998; McMichael et al ., 1998). UspA1 and UspA2 share an overall structural similarity of ≈ 43%.…”

Section: Introductionmentioning

confidence: 99%

“…UspA1 and UspA2 share an overall structural similarity of ≈ 43%. UspA1 proteins of distinct strains exhibit some structural variations, but they share a similar C‐terminal region, which is distinct from that of UspA2 proteins (Aebi et al ., 1997; McMichael et al ., 1998; Cope et al ., 1999). In addition, hybrid proteins containing both UspA1 and UspA2 domains have been described (Lafontaine et al ., 2000).…”

Section: Introductionmentioning

confidence: 99%

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A novel cell-binding mechanism of Moraxella catarrhalis ubiquitous surface protein UspA: specific targeting of the N-domain of carcinoembryonic antigen-related cell adhesion molecules by UspA1

Hill

Virji²

2003

Molecular Microbiology

133

166

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A novel cell-binding mechanism of Moraxella catarrhalis ubiquitous surface protein UspA: specific targeting of the N-domain of carcinoembryonic antigen-related cell adhesion molecules by UspA1

Hill

Virji²

2003

Molecular Microbiology

133

166

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“…The recently recognized 'oligomeric coiled-coil adhesin' (Oca) family belongs to the wider family of trimeric autotransporter adhesins (TAAs) characterized by the ability to form highly stable trimers on the bacterial surface and by a common mechanism of secretion, which is linked to their trimerization (Surana et al, 2004;Cotter et al, 2005;Linke et al, 2006). To date, all of them appear to have adhesive activity that is involved in mediating bacterial interaction with either host cells or extracellular matrix (ECM) proteins and in some cases in inducing invasion of target cells (Yang and Isberg, 1993;McMichael et al, 1998;Eitel and Dersch, 2002;Laarmann et al, 2002;Ray et al, 2002;Roggenkamp et al, 2003;Li et al, 2004;Riess et al, 2004;Zhang et al, 2004;Capecchi et al, 2005;Girard and Mourez, 2006;Heise and Dersch, 2006;Scarselli et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

HadA is an atypical new multifunctional trimeric coiled-coil adhesin ofHaemophilus influenzaebiogroupaegyptius, which promotes entry into host cells

Serruto

Spadafina

Scarselli

et al. 2009

Cellular Microbiology

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SummaryThe Oca (Oligomeric coiled-coil adhesin) family is a subgroup of the bacterial trimeric autotransporter adhesins, which includes structurally related proteins, such as YadA of Yersinia enterocolitica and NadA of Neisseria meningitidis. In this study, we searched in silico for novel members of this family in bacterial genomes and identified HadA (Haemophilus adhesin A), a trimeric autotransporter expressed only by Haemophilus influenzae biogroup aegyptius causing Brazilian purpuric fever (BPF), a fulminant septicemic disease of children. By comparative genomics and sequence analysis we predicted that the hadA gene is harboured on a mobile genetic element unique to BPF isolates. Biological analysis of HadA in the native background was limited because this organism is not amenable to genetic manipulation. Alternatively, we demonstrated that expression of HadA confers to a non-invasive Escherichia coli strain the ability to adhere to human cells and to extracellular matrix proteins and to induce in vitro bacterial aggregation and microcolony formation. Intriguingly, HadA is predicted to lack the typical N-terminal head domain of Oca proteins generally associated with cellular receptor binding. We propose here a structural model of the HadA coiled-coil stalk and show that the N-terminal region is still responsible of the binding activity and a KGD motif plays a role. Interestingly, HadA promotes bacterial entry into mammalian cells. Our results show a cytoskeleton re-arrangement and an involvement of clathrin in the HadA-mediated internalization. These data give new insights on the structure-function relationship of oligomeric coiled-coil adhesins and suggest a potential role of this protein in the pathogenesis of BPF.

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“…Despite M. catarrhalis being acknowledged as a human pathogen, only a few reports exist about its specific virulence factors. It is interesting that M. catarrhalis hampers the host innate immune system by conferring serum resistance [5,6]. We have recently shown that M. catarrhalis interferes with the complement activation pathway by binding C4b-binding protein (C4BP) and C3 to UspA1 and UspA2 [7,8].…”

Section: Introductionmentioning

confidence: 99%

The IgD-binding domain of the Moraxella IgD-binding protein MID (MID962-1200) activates human B cells in the presence of T cell cytokines

Nordström

Jendholm

Samuelsson

et al. 2005

Journal of Leukocyte Biology

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Moraxella catarrhalis immunoglobulin D (IgD)‐binding protein (MID) is an outer membrane protein with specific affinity for soluble and cell‐bound human IgD. Here, we demonstrate that mutated M. catarrhalis strains devoid of MID show a 75% decreased activation of human B cells as compared with wild‐type bacteria. In contrast to MID‐expressing Moraxella, the MID‐deficient Moraxella mutants did not bind to human CD19+ IgD+ B cells. The smallest MID fragment with preserved IgD‐binding capacity comprises 238 amino acids (MID962‐1200). To prove the specificity of MID962‐1200 for IgD, a Chinese hamster ovary (CHO) cell line expressing membrane‐anchored human IgD was manufactured. MID962‐1200 bound strongly to the recombinant IgD on CHO cells. Moreover, MID962‐1200 stimulated peripheral blood lymphocyte (PBL) proliferation 5‐ and 15‐fold at 0.1 and 1.0 μg/ml, respectively. This activation could be blocked completely by antibodies directed against the CD40 ligand (CD154). MID962‐1200 also activated purified B cells in the presence of interleukin (IL)‐2 or IL‐4. An increased IL‐6 production was seen after stimulation with MID962‐1200, as revealed by a human cytokine protein array. MID962‐1200 fused to green fluorescent protein (GFP) bound to human B cells and activated PBL to the same degree as MID962‐1200. Taken together, MID is the only IgD‐binding protein in Moraxella. Furthermore, the novel T cell‐independent antigen MID962‐1200 may, together with MID962‐1200–GFP, be considered as promising reagents in the study of IgD‐dependent B cell activation.

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Isolation and Characterization of Two Proteins fromMoraxella catarrhalis That Bear a Common Epitope

Cited by 14 publications

References 0 publications

A novel cell-binding mechanism of Moraxella catarrhalis ubiquitous surface protein UspA: specific targeting of the N-domain of carcinoembryonic antigen-related cell adhesion molecules by UspA1

A novel cell-binding mechanism of Moraxella catarrhalis ubiquitous surface protein UspA: specific targeting of the N-domain of carcinoembryonic antigen-related cell adhesion molecules by UspA1

HadA is an atypical new multifunctional trimeric coiled-coil adhesin ofHaemophilus influenzaebiogroupaegyptius, which promotes entry into host cells

The IgD-binding domain of the Moraxella IgD-binding protein MID (MID962-1200) activates human B cells in the presence of T cell cytokines

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