Binding of hemolin to bacterial lipopolysaccharide and lipoteichoic acid. An immunoglobulin superfamily member from insects as a pattern-recognition receptor

Yu, Xiao‐Qiang; Kanost, Michael R.

doi:10.1046/j.1432-1327.2002.02830.x

Cited by 18 publications

(33 citation statements)

References 23 publications

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“…5D). Previously, it was shown that hemolin from Manduca sexta has two binding sites for LPS, one that interacts with the lipidic portion and one that interacts with the outer core carbohydrates of LPS (17). Moreover, it was shown that another hemolin, H. cecropia hemolin, is a calcium-binding protein (47).…”

Section: Discussionmentioning

confidence: 99%

“…Hemolin is a bacteria-inducible immunoglobulinlike protein whose role in insect immunity has been better studied. In the last 2 decades, independent studies have demonstrated that hemolin proteins are multifunctional molecules involved in a diverse range of cell interaction and are able to (a) bind lipopolysaccharides and be up-regulated in hemolymph during infections (15)(16)(17); (b) be up-regulated during metamorphosis (18,19); (c) promote opsonin-like effects, such as increased cell adhesion and phagocytosis (20,21); (d) agglutinate bacterial cells (17,22); (e) bind to hemocytes and inhibit their aggregation (15,20,22,23); and (f) regulate embryonic development (24,25).…”

mentioning

confidence: 99%

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Losac, the First Hemolin that Exhibits Procogulant Activity through Selective Factor X Proteolytic Activation

Alvarez-Flores

Furlin

Ramos

et al. 2011

Journal of Biological Chemistry

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Envenoming by the contact of human skin with Lonomia obliqua caterpillars promotes a hemorrhagic syndrome characterized by a consumptive coagulopathy. Losac (Lonomia obliqua Stuart factor activator) is a component of the bristle of L. obliqua that is probably partially responsible for the observed syndrome because it activates factor X and is recognized by an effective antilonomic serum. Here we unveil the proteolytic activity of Losac and demonstrate the feasibility of its recombinant production. On the other hand, Losac has no homology to known proteases, but it can be inhibited by PMSF, a serine protease inhibitor. Instead, it shows closer homology to members of the hemolin family of proteins, a group of cell adhesion molecules. The recombinant protein (rLosac) shortened the coagulation time of normal and deficient plasmas, whereas it was ineffective in factor X-deficient plasma unless reconstituted with this protein. rLosac was able to activate factor X in a dose-and time-dependent manner but not ␥-carboxyglutamic acid domainless factor X. Moreover, phospholipids and calcium ions increased rLosac activity. Also, rLosac had no effect on fibrin or fibrinogen, indicating its specificity for blood coagulation activation. Linear double reciprocal plots indicate that rLosac follows a Michaelis-Menten kinetics. Cleavage of factor X by rLosac resulted in fragments that are compatible with those generated by RVV-X (a well known factor X activator). Together, our results validate Losac as the first protein from the hemolin family exhibiting procoagulant activity through selective proteolysis on coagulation factor X.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Losac, the First Hemolin that Exhibits Procogulant Activity through Selective Factor X Proteolytic Activation

Alvarez-Flores

Furlin

Ramos

et al. 2011

Journal of Biological Chemistry

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“…A clear interaction between hemolin and LPS was found in 1997 [44]. This was followed up by Kanost et al, who demonstrated its binding to lipoteichoic acid [45]. Hemolin has been proposed to function as an opsonin and participate in phagocytosis, melanization, and to some extent antiviral processes [46,47].…”

Section: (A) An Immunoglobulin-like Immune Proteinmentioning

confidence: 94%

Towards a paradigm shift in innate immunity—seminal work by Hans G. Boman and co-workers

Faye

Lindberg

2016

Phil. Trans. R. Soc. B

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“…Due to their adhesion properties, some hemolins have been involved in the cell adhesion mechanisms. In the last two decades independent studies demonstrated that hemolins are multifunctional molecules involved in a diverse range of cell interaction [104][105][106][107][108][109][110]. The high identity among Losac and hemolins suggests that Losac could also assume some of these functions in L. obliqua.…”

Section: Molecular Cloning and Heterologous Expression Of Losacmentioning

confidence: 99%

Toxins from Lonomia obliqua — Recombinant Production and Molecular Approach

Chudzinski-Tavassi¹,

Alvarez-Flores²,

Carrijo-Carvalho³

et al. 2013

An Integrated View of the Molecular Recognition and Toxinology - From Analytical Procedures to Biomedical Applications

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Binding of hemolin to bacterial lipopolysaccharide and lipoteichoic acid. An immunoglobulin superfamily member from insects as a pattern-recognition receptor

Cited by 18 publications

References 23 publications

Losac, the First Hemolin that Exhibits Procogulant Activity through Selective Factor X Proteolytic Activation

Losac, the First Hemolin that Exhibits Procogulant Activity through Selective Factor X Proteolytic Activation

Towards a paradigm shift in innate immunity—seminal work by Hans G. Boman and co-workers

Toxins from Lonomia obliqua — Recombinant Production and Molecular Approach

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