Infectious Disease Antigens

*Antigens associated with the following infectious diseases*

Anaplasmosis

Product Code Quantity Product Name Downloads Data Sheet
45600
45601
0.1 mg
1.0 mg

Anaplasma phagocytophilum Msp5

The zoonotic disease human granulocytic anaplasmosis is a tick-borne rickettsial disease caused by the Gram-negative bacterium Anaplasma phagocytophilum. Major surface protein Msp5 is conserved among the Anaplasma species and expressed in the salivary glands of infected ticks.
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45500
45501
0.1 mg
1.0 mg

Anaplasma phagocytophilum p44

Pathogenesis of human granulocytic anaplasmosis (HGA) is an issue of global concern. A. phagocytophilum p44, a member of the outer membrane protein superfamily (OMP1/Msp2/p44), is a well-known serodiagnostic protein for HGA. The protein is thought to allow the bacterium to adhere to the host cell and avoid host immune surveillance.
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Babesiosis

Product Code Quantity Product Name Downloads Data Sheet
44200
44201
0.1 mg
1.0 mg

Babesia microti IRA

Babesia microti, the causative agent of human babesiosis, is primarily transmitted by ticks of the genus Ixodes. Upon transmission, B. microti infects and replicates within erythrocytes. The cytoplasmic B. microti interspersed repeat antigen (IRA) comprises three distinct blocks of repetitive amino acids and is an immunodominant protein.
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44100
44101
0.1 mg
1.0 mg

Babesia microti p32

Babesiois is caused by the apicomplexan parasite Babesia microti that has been identified in North America and several European countries. Besides tick bites, blood transfusions are considered a potential route for transmission. A 32-kDa secretory protein (p32) has been identified to be immunogenic during B. microti infections.
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Borreliosis / Lyme Disease / Relapsing Fever

Product Code Quantity Product Name Downloads Data Sheet
41100
41101
0.1 mg
1.0 mg

Borreliella afzelii BmpA

The Gram-negative bacterium Borreliella afzelii is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. B. afzelii basic membrane protein A (BmpA) localizes to the outer membrane of this bacterium and binds to laminin in the host’s extracellular matrix.
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40900
40901
0.1 mg
1.0 mg

Borreliella afzelii DbpA

The Gram-negative bacterium Borreliella afzelii is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. Decorin is a proteoglycan on the surface of human cells to which B. burgdorferi binds via its adhesin decorin binding protein A (DbpA).
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41000
41001
0.1 mg
1.0 mg

Borreliella afzelii OspA

The Gram-negative bacterium Borreliella afzelii is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. Outer surface protein A (OspA) is one of the major proteins in the bacterium's outer membrane.
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41800
41801
0.1 mg
1.0 mg

Borreliella afzelii OspC

The Gram-negative bacterium Borreliella afzelii is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. As reflected by its name, outer surface protein C (OspC) is abundantly expressed on the bacterium’s outer surface.
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42300
42301
0.1 mg
1.0 mg

Borreliella afzelii p100

The Gram-negative bacterium Borreliella afzelii is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. B. afzelii p100 is an important immunodominant protein.
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42700
42701
0.1 mg
1.0 mg

Borreliella bavariensis DbpA

Borreliella bavariensis is one of the pathogens of the Borreliella burgdorferi sensu lato complex and causative agent of Lyme disease, mainly in Europe. Decorin binding protein A (DbpA), also referred to as Osp17 or p17, has a molecular size of approximately 17 kDa and is expressed during the mammalian phase of infection. DbpA is associated with binding of the pathogen to host collagen-associated proteoglycan decorin.
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40700
40701
0.1 mg
1.0 mg

Borreliella bavariensis p58

The Gram-negative bacterium Borreliella bavariensis is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. The function of p58 is still widely elusive, but it shares a functional domain usually found in periplasmic oligopeptide-binding proteins (Opp). Therefore, p58 is suggested to be involved in the transmembrane transport of solutes and is alternatively known as OppA-2.
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41400
41401
0.1 mg
1.0 mg

Borreliella bavariensis VlsE1

The Gram-negative bacterium Borreliella bavariensis is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. Variable major protein like sequence E1 protein (VlsE1) is a borrelial surface protein suggested to be involved in immune evasion.
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40500
40501
0.1 mg
1.0 mg

Borreliella burgdorferi BmpA

The Gram-negative bacterium Borreliella burgdorferi is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. B. burgdorferi basic membrane protein A (BmpA) localizes to the bacterium's outer membrane and binds to laminin in the host’s extracellular matrix. BmpA's alternative name p39 is indicative of its electrophoretic mobility.
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40400
40401
0.1 mg
1.0 mg

Borreliella burgdorferi DbpA

The Gram-negative bacterium Borreliella burgdorferi is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. Decorin is a proteoglycan on the surface of human cells to which B. burgdorferi binds via its adhesin decorin binding protein A (DbpA). In electrophoretic analyses, DbpA from B. burgdorferi lysates migrates like a 17 kDa protein leading to its alternative name p17.
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40600
40601
0.1 mg
1.0 mg

Borreliella burgdorferi DbpB

The Gram-negative bacterium Borreliella burgdorferi is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. Decorin is a proteoglycan on the surface of human cells to which B. burgdorferi binds via its adhesin decorin binding protein B (DbpB).
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41300
41301
0.1 mg
1.0 mg

Borreliella burgdorferi NapA

The Gram-negative bacterium Borreliella burgdorferi is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. B. burgdorferi neutrophil activating protein A (NapA) interferes with the host’s immune system by inducing a humoral immune response.
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41200
41201
0.1 mg
1.0 mg

Borreliella burgdorferi OspA

The Gram-negative bacterium Borreliella burgdorferi is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. Outer surface protein A (OspA) is one of the major proteins in the outer membrane of this bacterium.
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40300
40301
0.1 mg
1.0 mg

Borreliella burgdorferi OspC

The Gram-negative bacterium Borreliella burgdorferi is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. As reflected by its name, outer surface protein C (OspC) is abundantly expressed on the bacterium’s outer surface.
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42500
42501
0.1 mg
1.0 mg

Borreliella burgdorferi p28

The protein Borreliella burgdorferi p28, also known as Oms28, is considered to play an important role in host-pathogen interaction of Lyme disease. First it was classified as an integral membrane protein, but investigation of the secondary structure suggests that it is a periplasmic protein associated with the outer membrane.
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42600
42601
0.1 mg
1.0 mg

Borreliella burgdorferi p30

The Gram-negative bacterium Borreliella burgdorferi is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. Immunofluorescence studies showed that antibodies against the outer surface protein p30 are recognized in Lyme borreliosis patients.
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40200
40201
0.1 mg
1.0 mg

Borreliella burgdorferi p41

The Gram-negative bacterium Borreliella burgdorferi is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. B. burgdorferi p41 is a protein found in the bacterium's flagella.
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41500
41501
0.1 mg
1.0 mg

Borreliella burgdorferi p45

The Gram-negative bacterium Borreliella burgdorferi is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. Although the lipoprotein Borreliella burgdorferi p45 localizes to the outer membrane of this bacterium, its function is still elusive.
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41600
41601
0.1 mg
1.0 mg

Borreliella burgdorferi p58

The Gram-negative bacterium Borreliella burgdorferi is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. Although the function of p58 is still widely elusive, the prediction of a functional domain usually found in periplasmic oligopeptide-binding proteins suggests a similar role in the transport of solutes across the cytoplasmic membrane.
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41700
41701
0.1 mg
1.0 mg

Borreliella burgdorferi p66

The Gram-negative bacterium Borreliella burgdorferi is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. Borreliella burgdorferi p66 is an outer membrane spanning protein alternatively named Oms66 that has a dual function in forming porins and being involved in host cell attachment by binding to αvβ3-integrins.
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40100
40101
0.1 mg
1.0 mg

Borreliella burgdorferi p100

The Gram-negative bacterium Borreliella burgdorferi is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. B. burgdorferi p100, also known as p83, p83/100 or p94, is an important immunodominant protein.
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45700
45701
0.1 mg
1.0 mg

Borreliella burgdorferi VlsE1

Variable major protein like sequence E1 protein (VlsE1) is a borrelial surface protein suggested to be the most sensitive protein for IgG antibody detection in all stages of Lyme disease. Please note that in the United States recombinant expression of this antigen and use in diagnostic assays is protected by several patents.
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42800
42801
0.1 mg
1.0 mg

Borreliella garinii DbpA

Considerable differences in the amino acid sequences exist among DbpA proteins of different Borreliella species, as it is known for other B. burgdorferi sensu lato proteins. Borreliella garinii DbpA shows the typical lipid anchor and decorin/glycoaminoglycon binding properties of a DbpA protein.
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41900
41901
0.1 mg
1.0 mg

Borreliella garinii OspC

The Gram-negative bacterium Borreliella garinii is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. As reflected by its name, outer surface protein C (OspC) is abundantly expressed on the bacterium’s outer surface.
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42400
42401
0.1 mg
1.0 mg

Borrelia miyamotoi GlpQ

B. miyamotoi is distantly related to B. burgdorferi and also transmitted by ticks of the genus Ixodes. In contrast to B. burgdorferi, B. miyamotoi encodes glycerophosphodiester phosphodiesterase (GlpQ), an enzyme that hydrolyzes deacylated phospholipids to glycerol-3-phosphate.
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42900
42901
0.1 mg
1.0 mg

Borreliella spielmanii DbpA

DbpA, also named p17 or Osp17, is a diagnostically relevant but heterogeneous protein among the human pathogenic B. burgdorferi sensu lato species. It has been shown that integration in serologic borreliosis assays significantly improves sensitivity of IgG and IgM detection in patient sera.
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40800
40801
0.1 mg
1.0 mg

Borreliella spielmanii OspC

The Gram-negative bacterium Borreliella spielmanii is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. As reflected by its name, outer surface protein C (OspC) is abundantly expressed on the bacterium’s outer surface.
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Candidiasis

Product Code Quantity Product Name Downloads Data Sheet
44800
44801
0.1 mg
1.0 mg

Candida albicans Bgl2

Candida albicans is a pathogenic commensal colonizing human skin and mucosal surfaces. However, imbalance of the controlled homeostasis can cause an infection called candidiasis. C. albicans Glucan 1,3-beta-glycolytic enzyme (Bgl2) is a cell wall localized glycosyltransferase implicated in assembly of the protective cell wall polysaccharides. Its deletion negatively affects the virulence of C. albicans.
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45300
45301
0.1 mg
1.0 mg

Candida albicans Enolase

In glycolysis, enolase catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate. This enzyme is synonymous with 2-phospho-D-glycerate hydrolyase and 2-phosphoglycerate dehydratase. It is localized in cytoplasm and cell wall of C. albicans.
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45400
45401
0.1 mg
1.0 mg

Candida albicans Hsp70

Heat shock protein 70 (Hsp 70, also named SSA1) is a molecular chaperon important for protein folding under heat shock conditions localized in cytoplasm or cell wall of the diploid, unicellular C. albicans. As its biological role in the cell wall is the adhesion to host cells, it is considered an important antigen in immunological diagnosis.
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44900
44901
0.1 mg
1.0 mg

Candida albicans Met6

Especially in immunocompromised individuals, C. albicans can cause systemic infections by entering the blood stream (candidaemia). C. albicans methionine synthase (Met6) is an essential enzyme implicated in the synthesis of methionine via transfer of a methyl group from tetrahydrofolate to homocysteine. In patients suffering from systemic candidiasis it is considered the major antigen.
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Erythema infectiosum

Product Code Quantity Product Name Downloads Data Sheet
48000
48001
0.1 mg
1.0 mg

Parvovirus B19 VLP VP2

Parvovirus B19 propagates primarily in erythroid progenitor cells and is the causative agent of erythema infectiosum. VP2 is the major structural protein of the viral capsid. DIARECT offers recombinant VP2 assembled into virus like particles (VLP).
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48100
48101
0.1 mg
1.0 mg

Parvovirus B19 VLP VP1/VP2 Co-Capsid

Parvovirus B19 propagates primarily in erythroid progenitor cells and is the causative agent of erythema infectiosum. The viral capsid comprises a major and a minor structural protein, named VP2 and VP1, respectively. DIARECT offers recombinant VP1 and VP2 co-assembled into virus like particles (VLP).
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Scarlet Fever

Product Code Quantity Product Name Downloads Data Sheet
44500
44501
0.1 mg
1.0 mg

Streptococcus pyogenes Arginine Deiminase (arcA)

Under glucose limiting conditions, Streptococcus pyogenes uses L-arginine as energy source. Arginine deiminase (arcA) hydrolyzing L-arginine into L-citrulline and ammonia is the first enzyme of this catabolic pathway. Initially, arcA has been known as streptococcal acid glycoprotein (SAGP), an inhibitor of peripheral blood mononuclear cell proliferation with arginine deiminase activity.
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44700
44701
0.1 mg
1.0 mg

Streptococcus pyogenes Streptolysin O (slo)

Extracellular protein streptolysin O is a key virulence factor of group A streptococci and belongs to the beta-barrel pore-forming exotoxin family called thiol-activated cholesterol-dependent cytolysins (CDCs). After secretion, it binds to the host erythrocyte membranes forming ring-like structures. The presence of cholesterol in the target membrane is required for pore formation which finally results in cytolysis.
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44600
44601
0.1 mg
1.0 mg

Streptococcus pyogenes Transketolase (tkt)

In the pentose phosphate pathway, the enzyme transketolase catalyzes two reactions contributing to the conversion of ribulose-5-phosphate into glyceraldehyde-3-phosphate and fructose-6-phosphate. In Streptococcus pyogenes, transketolase has been found to be associated with the cell wall and exposed to the surface.
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Yersiniosis

Product Code Quantity Product Name Downloads Data Sheet
43000
43001
0.1 mg
1.0 mg

Yersinia enterocolitica (O:8) YopM

Yersinia enterocolitica is a Gram-negative coccobacillus of which pathogenic serogroups, e.g. O:8, have been identified. Yersinia outer proteins (Yops) are key virulence factors during the infection of host cells. YopM is injected into the host cell’s cytosol where it interferes with the regulation of translation by activating ribosomal S6 kinase.
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43100
43101
0.1 mg
1.0 mg

Yersinia enterocolitica (O:9) LcrV

Yersinia enterocolitica serogroup O:9 is a causative agent of yersiniosis, a food-borne gastro-intestinal infection in humans. As part of the bacterial translocation apparatus, low calcium response V antigen (LcrV) is necessary for the secretion of Yersinia outer proteins (Yops) involved in host cell infection.
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43200
43201
0.1 mg
1.0 mg

Yersinia enterocolitica (O:9) YopB

Virulent isolates of Yersinia enterocolitica have been identified to cause gastroenteritis: yersiniosis. Yop B serves as an adapter protein and is necessary in pore-formation during infection. This enables delivery of Yop effectors into host cells.
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43300
43301
0.1 mg
1.0 mg

Yersinia enterocolitica (O:9) YopD

Upon the consumption of raw or undercooked contaminated food, humans can become infected with bacteria of the Yersinia enterocolitica serogroup O:9. During this infection, bacterial proteins are secreted to form pores in the host cell’s plasma membrane. Yersinia outer protein D (YopD) serves as an adapter protein in this process.
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43700
43701
0.1 mg
1.0 mg

Yersinia enterocolitica (O:9) YopE

A key virulence factor of pathogenic Yersinia enterocolitica strains is a plasmid-encoded type III secretion system, through which Yersinia outer proteins (Yops) are injected into the host cell. Yop E, a GTPase activation protein controls pore formation by activating small Rho GTPase, leading to inhibition of actin polymerization.
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43400
43401
0.1 mg
1.0 mg

Yersinia enterocolitica (O:9) YopH

To successfully infect human gastrointestinal cells, pathogenic Yersinia enterocolitica secrete and translocate various so-called Yersinia outer proteins (Yops) into host cells. Following translocation, the protein tyrosine phosphatase YopH (synonyme Yop51) affects signaling cascades by dephosphorylating host cell proteins.
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43500
43501
0.1 mg
1.0 mg

Yersinia enterocolitica (O:9) YopM

Besides Yersinia enterocolitica serogroups O:3 and O:8, serogroup O:9 is also pathogenic to humans and able to establish a gastrointestinal infection. During this process, Yersinia outer protein M (YopM) is actively injected into human cells where it activates ribosomal S6 kinase to manipulate host cell translation.
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43600
43601
0.1 mg
1.0 mg

Yersinia enterocolitica (O:9) YopN

Upon contact with a host cell, bacteria of the Yersinia enterocolitica serogroup O:9 secrete several effector proteins to establish an infection in humans. Yersinia outer proteins (Yops) are key virulence factors during the infection of host cells. YopN is involved in the prevention of the secretion of other Yops prior to contact to a host cell.
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