Multiple-routes of complement activation by Mycobacterium bovis BCG

Lack, Nathan A.; Krarup, Anders; Fedorova, Marina; Sim, Edith; Sim, Robert B.

doi:10.1016/j.molimm.2008.08.218

Cited by 11 publications

(18 citation statements)

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“…L-ficolin has a broad affinity for microorganisms and parasites, e.g. S. typhimurium TV119, S. aureus, S. pneumoniae (Krarup et al, 2005), Trypanosom cruzi (Cestari Idos et al, 2009), Mycobacterium bovis (Carroll et al, 2009), Giardia intestinalis (Evans-Osses The assembled model of a MASP protease in complex with a tetramer of MBL trimers, see the supplementary text for description of procedure. The plane at the bottom approximates the glycan layer.…”

Section: L-ficolinmentioning

confidence: 99%

Toward a structure-based comprehension of the lectin pathway of complement

Kjær

Thiel

Andersen

2013

Molecular Immunology

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To initiate the lectin pathway of complement pattern recognition molecules bind to surface-linked carbohydrates or acetyl groups on pathogens or damaged self-tissue. This leads to activation of the serine proteases MASP-1 and MASP-2 resulting in deposition of C4 on the activator and assembly of the C3 convertase. In addition MASP-3 and the non-catalytic MAp19 and MAp44 presumably play regulatory functions, but the exact function of the MASP-3 protease remains to be established. Recent functional studies have significantly advanced our understanding of the molecular events occurring as activation progresses from pattern recognition to convertase assembly. Furthermore, atomic structures derived by crystallography or solution scattering of most proteins acting in the lectin pathway and two key complexes have become available. Here we integrate the current functional and structural knowledge concerning the lectin pathway proteins and derive overall models for their glycan bound complexes. These models are used to discuss cis- versus trans-activation of MASP proteases and the geometry of C4 deposition occurring on glycans in the lectin pathway.

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Section: L-ficolinmentioning

confidence: 99%

Toward a structure-based comprehension of the lectin pathway of complement

Kjær

Thiel

Andersen

2013

Molecular Immunology

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“…Mtb can activate the classical and alternate pathways by binding C3. This enables complement to perform its major functions-microbial opsonization, microbial cell lysis through the formation of the attack complex and leukocyte recruitment by eliciting chemokine secretion [7,17].…”

Section: The Encounter Of Mtb With the Innate Immune Systemmentioning

confidence: 99%

The Immune Response to Mycobacterium tuberculosis Infection in Humans

Handzel¹

2013

Tuberculosis - Current Issues in Diagnosis and Management

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“…The pathways consist of approximately 30 proteins, both circulating and membrane bound, with regulators at strategic locations. 3 Although complement remained unexplored for a long time after its discovery, different relevant proteins have been identified over time. More recently, complement research has become a dynamic area of study with discoveries of novel functions, and there is an urgency to identify effective complement therapies.…”

mentioning

confidence: 99%