The Moraxella IgD-binding protein MID/Hag is an oligomeric autotransporter

Hallström, Teresia; Müller, Shirley A.; Mörgelin, Matthias; Möllenkvist, Andrea; Forsgren, Arne; Riesbeck, Kristian

doi:10.1016/j.micinf.2007.12.015

Cited by 15 publications

(16 citation statements)

References 30 publications

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“…Interestingly, TEM revealed that NID on E. coli retained a characteristic structure that was similar to native MID at the surface of M. catarrhalis. 4 Taken together, our results demonstrate that a chimeric NID molecule can be constructed and expressed at the E. coli surface. A cartoon with the proposed trimeric structure of NID is shown in Figure 1D.…”

supporting

confidence: 59%

“…3 Using ultracentrifugation and gel electrophoresis we showed that MID 962-1200 exists as a trimer and that this configuration is crucial for optimal IgD-binding capacity. 4 The specific binding of MID to soluble IgD and the IgD B cell receptor (BCR) leads to induction and proliferation of human B lymphocytes, resulting in production of non-specific IgGs, thereby regulating the hostpathogen interaction. 2,5 Release of outer membrane vesicles (OMV) is another mechanism by which Gram-negative bacteria regulate their interaction with the host.…”

mentioning

confidence: 99%

“…Since MID has been demonstrated to bind the IgD BCR on B cells as well as to stimulate those cells to proliferate, 4 we wanted to analyze whether NID had the same functional property. Bacteria carrying NID were labeled with FITC and incubated with human PBLs.…”

mentioning

confidence: 99%

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A fusion protein derived fromMoraxella catarrhalisandNeisseria meningitidisaimed for immune modulation of human B cells

Mukherjee

Singh

Bayrak

et al. 2015

Human Vaccines & Immunotherapeutics

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confidence: 59%

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confidence: 99%

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A fusion protein derived fromMoraxella catarrhalisandNeisseria meningitidisaimed for immune modulation of human B cells

Mukherjee

Singh

Bayrak

et al. 2015

Human Vaccines & Immunotherapeutics

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“…The M. catarrhalis UspAs and MID/Hag are classified as trimeric autotransporters, also known as oligomeric coiled-coil adhesins (Oca proteins) (30,56,70,83). The group of trimeric autotransporters is a large protein family consisting of virulence factors of diverse pathogenic gram-negative bacteria, such as the YadA protein of Yersinia spp.…”

Section: Adhesion and Major Ompsmentioning

confidence: 99%

Molecular Aspects ofMoraxella catarrhalisPathogenesis

Vries

Bootsma

Hays

et al. 2009

Microbiol Mol Biol Rev

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SUMMARY In recent years, Moraxella catarrhalis has established its position as an important human mucosal pathogen, no longer being regarded as just a commensal bacterium. Further, current research in the field has led to a better understanding of the molecular mechanisms involved in M. catarrhalis pathogenesis, including mechanisms associated with cellular adherence, target cell invasion, modulation of the host's immune response, and metabolism. Additionally, in order to be successful in the host, M. catarrhalis has to be able to interact and compete with the commensal flora and overcome stressful environmental conditions, such as nutrient limitation. In this review, we provide a timely overview of the current understanding of the molecular mechanisms associated with M. catarrhalis virulence and pathogenesis.

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“…Previously, we noticed a similar double-fold in a large TAA, i.e., Moraxella catarrhalis IgD binding protein (MID). In parallel to Hsf, MID is also an extraordinary large protein (Hallstrom et al, 2008). Interestingly, the Hsf homologue Hia having 70% similarity is present in NTHi, and is only 1000 amino acids in length and not bended and twisted like Hsf .…”

Section: Discussionmentioning

confidence: 99%

Haemophilus influenzae surface fibril (Hsf) is a unique twisted hairpin-like trimeric autotransporter

Singh

Jubair

Mörgelin

et al. 2015

International Journal of Medical Microbiology

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The Haemophilus surface fibril (Hsf) is an extraordinary large (2413 amino acids) trimeric autotransporter, present in all encapsulated Haemophilus influenzae. It contributes to virulence by directly functioning as an adhesin. Furthermore, Hsf recruits the host factor vitronectin thereby inhibiting the host innate immune response resulting in enhanced survival in serum. Here we observed by electron microscopy that Hsf appears as an 100 nm long fibril at the bacterial surface albeit the length is approximately 200 nm according to a bioinformatics based model. To unveil this discrepancy, we denaturated Hsf at the surface of Hib by using guanidine hydrochloride (GuHCl). Partial denaturation induced in the presence of GuHCl unfolded the Hsf molecules, and resulted in an increased length of fibres in comparison to the native trimeric form. Importantly, our findings were also verified by E. coli expressing Hsf at its surface. In addition, a set of Hsf-specific peptide antibodies also indicated that the N-terminal of Hsf is located near the C-terminal at the base of the fibril. Taken together, our results demonstrated that Hsf is not a straight molecule but is folded and doubled over. This is the first report that provides the unique structural features of the trimeric autotransporter Hsf. Highlights Trimeric autotransporters are important virulence factors of Gram negative bacteria, and have a "lollipop-shape" structure or straight trimeric strand.  Haemophilus surface fibril is involved in adherence to host epithelium and for recruitment of vitronectin.  Here we show for the first time that Haemophilus surface fibril has a twisted hairpin-like structure.

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The Moraxella IgD-binding protein MID/Hag is an oligomeric autotransporter

Cited by 15 publications

References 30 publications

A fusion protein derived fromMoraxella catarrhalisandNeisseria meningitidisaimed for immune modulation of human B cells

A fusion protein derived fromMoraxella catarrhalisandNeisseria meningitidisaimed for immune modulation of human B cells

Molecular Aspects ofMoraxella catarrhalisPathogenesis

Haemophilus influenzae surface fibril (Hsf) is a unique twisted hairpin-like trimeric autotransporter

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