Ficolin-3 activity towards the opportunistic pathogen, Hafnia alvei

Michalski, Mateusz; Świerzko, Anna St.; Łukasiewicz, Jolanta; Man-Kupisinska, Aleksandra; Karwaciak, Iwona; Przygodzka, Patrycja; Cedzyński, Maciej

doi:10.1016/j.imbio.2014.08.012

Cited by 22 publications

(21 citation statements)

References 37 publications

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“…The key distinguishing features of our method for isolation of native ficolin-3 complexes from plasma are: (i) an affinity chromatography step using LPS-derived O-PS 1200, a specific ligand for ficolin-3 from H . alvei PCM 1200 that we have previously shown is effective for measuring ficolin-3 concentration and activity [ 12 , 21 , 39 , 51 – 54 ] and (ii) yeast and l -Fuc incubation step to eliminate MBL. The O-PS 1200 ligand exclusively interacted with ficolin-3 and showed no binding with ficolin-1, ficolin-2 and MBL and relatively weak with Ig ( S3 and S4 Figs).…”

Section: Discussionmentioning

confidence: 99%

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A New Ligand-Based Method for Purifying Active Human Plasma-Derived Ficolin-3 Complexes Supports the Phenomenon of Crosstalk between Pattern-Recognition Molecules and Immunoglobulins

et al. 2016

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Despite recombinant protein technology development, proteins isolated from natural sources remain important for structure and activity determination. Ficolins represent a class of proteins that are difficult to isolate. To date, three methods for purifying ficolin-3 from plasma/serum have been proposed, defined by most critical step: (i) hydroxyapatite absorption chromatography (ii) N-acetylated human serum albumin affinity chromatography and (iii) anti-ficolin-3 monoclonal antibody-based affinity chromatography. We present a new protocol for purifying ficolin-3 complexes from human plasma that is based on an exclusive ligand: the O-specific polysaccharide of Hafnia alvei PCM 1200 LPS (O-PS 1200). The protocol includes (i) poly(ethylene glycol) precipitation; (ii) yeast and l-fucose incubation, for depletion of mannose-binding lectin; (iii) affinity chromatography using O-PS 1200-Sepharose; (iv) size-exclusion chromatography. Application of this protocol yielded average 2.2 mg of ficolin-3 preparation free of mannose-binding lectin (MBL), ficolin-1 and -2 from 500 ml of plasma. The protein was complexed with MBL-associated serine proteases (MASPs) and was able to activate the complement in vitro. In-process monitoring of MBL, ficolins, and total protein content revealed the presence of difficult-to-remove immunoglobulin G, M and A, in some extent in agreement with recent findings suggesting crosstalk between IgG and ficolin-3. We demonstrated that recombinant ficolin-3 interacts with IgG and IgM in a concentration-dependent manner. Although this association does not appear to influence ficolin-3-ligand interactions in vitro, it may have numerous consequences in vivo. Thus our purification procedure provides Ig-ficolin-3/MASP complexes that might be useful for gaining further insight into the crosstalk and biological activity of ficolin-3.

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Section: Discussionmentioning

confidence: 99%

“…pneumotropica , E . coli ) [ 21 , 13 ], antifungal ( A . fumigatus ) [ 14 ], antiviral (influenza A virus) [ 15 ], and antiparasite activity ( Trypanosoma cruzi , Giardia intestinalis ) [ 16 , 17 ].…”

Section: Introductionmentioning

confidence: 99%

A New Ligand-Based Method for Purifying Active Human Plasma-Derived Ficolin-3 Complexes Supports the Phenomenon of Crosstalk between Pattern-Recognition Molecules and Immunoglobulins

et al. 2016

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“…44 Interaction of H-ficolin with LPS of H. alvei inhibits toll-like receptor 4 (TLR4)/MD-2/cluster of differentiation 4 activation of the nuclear factor kappa-light-chainenhancer of activated B cells (NFjB) transcription factor. 45 Like L-ficolin, the FBG domain of H-ficolin binds to apoptotic cells and necrotic cells and activates opsonization; however, H-ficolin does not bind to nucleic acids and it is unknown what the ligand is in this context. 46 An H-ficolin variant exists where a frameshift in exon 5 (Leu117fs) leads to complete deletion of the FBG domain of this protein.…”

Section: Patterns [Damps]mentioning

confidence: 99%

Fibrinogen-Related Proteins in Tissue Repair: How a Unique Domain with a Common Structure Controls Diverse Aspects of Wound Healing

Zuliani-Alvarez

Midwood

2015

Advances in Wound Care

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Fibrinogen-related proteins (FRePs) comprise an intriguing collection of extracellular molecules, each containing a conserved fibrinogen-like globe (FBG). This group includes the eponymous fibrinogen as well as the tenascin, angiopoietin, and ficolin families. Many of these proteins are upregulated during tissue repair and exhibit diverse roles during wound healing. An increasing body of evidence highlights the specific expression of a number of FRePs following tissue injury and infection. Upon induction, each FReP uses its FBG domain to mediate quite distinct effects that contribute to different stages of tissue repair, such as driving coagulation, pathogen detection, inflammation, angiogenesis, and tissue remodeling. Despite a high degree of homology among FRePs, each contains unique sequences that enable their diversification of function. Comparative analysis of the structure and function of FRePs and precise mapping of regions that interact with a variety of ligands has started to reveal the underlying molecular mechanisms by which these proteins play very different roles using their common domain. Fibrinogen has long been used in the clinic as a synthetic matrix serving as a scaffold or a delivery system to aid tissue repair. Novel therapeutic strategies are now emerging that harness the use of other FRePs to improve wound healing outcomes. As we learn more about the underlying mechanisms by which each FReP contributes to the repair response, specific blockade, or indeed potentiation, of their function offers real potential to enable regulation of distinct processes during pathological wound healing.

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“…FCN3, also known as H‐ficolin or Hakata antigen, is a complement‐activating pattern recognition molecule, member of the ficolin/opsonin p35 family and present in serum (Michalski et al . ). FCN3 possesses an N ‐terminal cysteine‐rich collagen‐like domain that forms complexes with mannose‐binding lectin‐associated serine proteases and activates the lectin pathway (Matsushita et al .…”

Section: Discussionmentioning

confidence: 97%

“…FCN3 seems to be an important component of innate immunity, showing a protective activity against bacterial pathogens (Michalski et al . ). Although the involvement of the immune response in OC pathogenesis remains unknown, it has been reported that the progression of OC lesions can lead to osteoarthritis (Scanzello et al .…”

Section: Discussionmentioning

confidence: 97%

Candidate gene analysis of osteochondrosis in Spanish Purebred horses

Sevane

Dunner

Boado³

et al. 2016

Animal Genetics

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Equine osteochondrosis (OC) is a frequent developmental orthopaedic disease with high economic impact on the equine industry and may lead to premature retirement of the animal as a result of chronic pain and lameness. The genetic background of OC includes different genes affecting several locations; however, these genetic associations have been tested in only one or few populations, lacking the validation in others. The aim of this study was to identify the genetic determinants of OC in the Spanish Purebred horse breed. For that purpose, we used a candidate gene approach to study the association between loci previously implicated in the onset and development of OC in other breeds and different OC locations using radiographic data from 144 individuals belonging to the Spanish Purebred horse breed. Of the 48 polymorphisms analysed, three single nucleotide polymorphisms (SNPs) located in the FAF1, FCN3 and COL1A2 genes were found to be associated with different locations of OC lesions. These data contribute insights into the complex gene networks underlying the multifactorial disease OC, and the associated SNPs could be used in a marker-assisted selection strategy to improve horse health, welfare and competitive lifespan.

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Ficolin-3 activity towards the opportunistic pathogen, Hafnia alvei

Cited by 22 publications

References 37 publications

A New Ligand-Based Method for Purifying Active Human Plasma-Derived Ficolin-3 Complexes Supports the Phenomenon of Crosstalk between Pattern-Recognition Molecules and Immunoglobulins

A New Ligand-Based Method for Purifying Active Human Plasma-Derived Ficolin-3 Complexes Supports the Phenomenon of Crosstalk between Pattern-Recognition Molecules and Immunoglobulins

Fibrinogen-Related Proteins in Tissue Repair: How a Unique Domain with a Common Structure Controls Diverse Aspects of Wound Healing

Candidate gene analysis of osteochondrosis in Spanish Purebred horses

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