Surface proteinaceous fibrils (fimbriae) on filamentous fungi

1988 ◽  
Vol 66 (12) ◽  
pp. 2474-2484 ◽  
Author(s):  
R. B. Gardiner ◽  
A. W. Day
Keyword(s):  
Filamentous Fungi ◽  
Surface Antigens ◽  
Surface Proteins ◽  
Diverse Group ◽  
Ustilago Violacea ◽  
Lower Eukaryotes

Proteinaceous fibrils (fimbriae) of 4–10 nm diam. have been described in several lower eukaryotes, including yeast-like fungi and certain algae. Antibodies prepared against the fimbriae of Ustilago violacea cross react with antigens present on the surface of these same organisms. In this paper we extend these observations to a diverse group of filamentous fungi, representing the major groups. These fungi also produce surface fibrils of 6–10 nm diam. and have surface antigens that cross react with the antibodies of U. violacea fimbriae. We conclude that surface proteins of a conserved type are common in the lower eukaryotes and that these may be manifested as surface fibrils of 4–10 nm diam. In some organisms these are extruded as numerous very long fimbriae (up to 30 μm); in others they may remain largely embedded in the wall or appear as a short fringe or as sparse longer fibrils.

Monoclonal antibodies against surface antigens of schistosomula of Schistosoma mansoni

Parasitology ◽  
1982 ◽  
Vol 84 (1) ◽  
pp. 65-82 ◽  
Author(s):  
D. W. Taylor ◽  
A. F. Butterworth
Keyword(s):  
Monoclonal Antibodies ◽  
Gel Electrophoresis ◽  
Primary Infection ◽  
Polyacrylamide Gel Electrophoresis ◽  
Apparent Molecular Weight ◽  
Surface Antigens ◽  
Soft Agar ◽  
Surface Proteins ◽  
Spleen Cells

SUMMARYMonoclonal antibodies have been produced after fusion of NS-1 murine myeloma cells with spleen cells from mice immunized either by chronic primary infection or with irradiated cercariae: in both cases, animals were challenged with live cercariae 7 days before fusion. The initial cultures were screened for anti-schistosomular antibodies both by a radioimmunoassay with whole schistosomulum extracts and by immunofluorescence. There was no correlation between the two techniques and subsequent screening was carried out by immunofluorescence. Cloning was carried out in soft agar and 7 cloned cell lines, from 5 initial cultures, were selected for detailed study. Products of 6 of these 7 lines were monoclonal, as judged by isoelectricfocusing of [35S]methionine-labelled supernatant fluids, and their binding to live schistosomula was specific. None of the antibodies showed detectable activity in mediating eosinophil- or complement-dependent damage to schistosomula in vitro. However, 2 antibodies were successfully used to isolate surface proteins with an apparent molecular weight of 24000 on SDS-polyacrylamide gel electrophoresis.

Nephrotoxic antiserum identifies a beta 1-integrin on rat glomerular epithelial cells

1992 ◽  
Vol 262 (6) ◽  
pp. F1083-F1091 ◽  
Author(s):  
Y. M. O'Meara ◽  
Y. Natori ◽  
A. W. Minto ◽  
D. J. Goldstein ◽  
E. C. Manning ◽  
...  
Keyword(s):  
Plasma Membranes ◽  
Direct Interaction ◽  
Surface Antigens ◽  
Surface Proteins ◽  
Glomerular Injury ◽  
Fibronectin Receptor ◽  
Glomerular Epithelial Cell ◽  
Beta 1 Integrin ◽  
Cell Matrix Interactions

A postulated mechanism of immune glomerular injury is a direct interaction between antibody and glomerular epithelial cell (GEC) surface antigens. To explore this hypothesis, we examined the interaction of the noncomplement-fixing gamma 2-subclass of sheep anti-rat nephrotoxic serum (NTS), which causes immediate complement- and neutrophil-independent proteinuria in vivo, with rat GECs in culture. Reactivity of NTS with GEC surface antigens was determined by positive immunofluorescence of GEC plasma membranes and by the ability of NTS-coated tissue culture wells to provide an adhesive substrate for GECs. NTS immunoprecipitated two proteins (135 and 118 kDa) from surface-labeled GECs. Proteins of similar molecular mass were precipitated by a polyclonal rabbit antibody that identifies the beta 1-integrin chain of the mouse fibronectin receptor (anti-FnR). In addition, NTS identified similarly sized bands on Western blot analysis of cell membranes from isolated rat glomeruli. Similar reactivity was eluted from the glomeruli of proteinuric rats injected with NTS. NTS significantly inhibited GEC adhesion to laminin, types I and IV collagen, and fibronectin and prevented GEC spreading on types I and IV collagen. Anti-FnR similarly inhibited GEC adhesion. Cell viability was not affected. These results show that NTS recognizes a pair of GEC surface proteins that have the characteristics of an alpha- and beta 1-integrin and, at low concentrations, disrupt cell-matrix interactions.

scholarly journals Immune response to stage-specific surface antigens of the parasitic nematode Trichinella spiralis.

1981 ◽  
Vol 154 (1) ◽  
pp. 210-215 ◽  
Author(s):  
M Philipp ◽  
P M Taylor ◽  
R M Parkhouse ◽  
B M Ogilvie
Keyword(s):  
Primary Infection ◽  
Time Course ◽  
Parasitic Nematode ◽  
Trichinella Spiralis ◽  
Serum Antibody ◽  
Surface Antigens ◽  
Surface Proteins ◽  
Infective Larvae ◽  
Intestinal Worms

Rats were infected with the nematode Trichinella spiralis and the primary serum antibody response to antigenic surface proteins of infective larvae, intestinal worms, and newborn larvae was studies. 1 wk after infection, the sera contained antibodies to surface antigens of both infective larvae and intestinal worms. These early sera, however, failed to react with newborn larvae surface antigens. In addition, adsorption of sera with living intestinal worms or infective larvae removed antibodies to surface antigens of the homologous stage only. Finally, the time-course of appearance of antibodies that mediate eosinophil adherence to the surface of each stage of the parasite. We concluded that in a primary infection in rats, the surface proteins of T. spiralis used in this study are antigenically stage specific. Furthermore, they could be targets for the stage-specific, antibody-dependent eosinophil-mediated destruction of this parasite, known to occur in vitro.

scholarly journals Mycobacterium bovis BCG Surface Antigens Expressed under the Granuloma-Like Conditions as Potential Inducers of the Protective Immunity

2019 ◽  
Vol 2019 ◽  
pp. 1-12 ◽  
Author(s):  
Yingyu Chen ◽  
Lia Danelishvili ◽  
Sasha J. Rose ◽  
Luiz E. Bermudez
Keyword(s):  
Mycobacterium Bovis ◽  
Recombinant Proteins ◽  
Protective Immunity ◽  
Bacterial Load ◽  
Surface Antigens ◽  
Surface Proteins ◽  
Host Cells ◽  
Biologically Relevant ◽  
Mucosal Cells ◽  
Potential Reservoir

Bovine tuberculosis (bTB) is a highly transmissible infection and remains of great concern as a zoonosis. The worldwide incidence of bTB is in rise, creating potential reservoir and increased infection risk for humans and animals. In attempts to identify novel surface antigens of Mycobacterium bovis as a proof-of-concept for potential inducers of protective immunity, we investigated surface proteome of M. bovis BCG strain that was cultured under the granuloma-like condition. We also demonstrated that the pathogen exposed to the biologically relevant environment has greater binding and invasion abilities to host cells than those of bacteria incubated under regular laboratory conditions. A total of 957 surface-exposed proteins were identified for BCG cultured under laboratory condition, whereas 1,097 proteins were expressed under the granuloma-like condition. The overexpression of Mb1524, Mb01_03198, Mb1595_p3681 (PhoU1 same as phoY1_1), and Mb1595_p0530 (HbhA) surface proteins in Mycobacterium smegmatis leads to increased binding and invasion to mucosal cells. We also examined the immunogenicity of purified recombinant proteins and tested M. smegmatis overexpressing these surface antigens for the induction of protective immunity in mice. Significantly high levels of specific IgA and IgG antibodies were observed in recombinant protein immunized groups by both inhalation and intraperitoneal (IP) routes, but only IP delivery induced high total IgA and IgG levels. We did not detect major differences in antibody levels in the M. smegmatis group that overexpressed surface antigens. In addition, the bacterial load was significantly reduced in the lungs of mice immunized with the combination of inhaled recombinant proteins. Our findings suggest that the activation of the mucosal immunity can lead to increased ability to confer protection upon M. bovis BCG infection.

Nanoscopic Localization of Surface-Exposed Antigens ofBorrelia burgdorferi

2015 ◽  
Vol 21 (3) ◽  
pp. 680-688 ◽  
Author(s):  
Leandro Lemgruber ◽  
Celso Sant’Anna ◽  
Caron Griffths ◽  
Yuri Abud ◽  
Musa Mhlanga ◽  
...  
Keyword(s):  
Lyme Disease ◽  
Super Resolution ◽  
Surface Antigens ◽  
Surface Proteins ◽  
Wide Field ◽  
Bacterial Surface ◽  
Outer Surface Proteins ◽  
Successful Infection ◽  
Vertebrate Hosts ◽  
Microscopy Techniques

AbstractBorrelia burgdorferisensu lato, the causative agent of Lyme disease, is transmitted to humans through the bite of infectedIxodesspp. ticks. Successful infection of vertebrate hosts necessitates sophisticated means of the pathogen to escape the vertebrates’ immune system. One strategy employed by Lyme disease spirochetes to evade adaptive immunity involves a highly coordinated regulation of the expression of outer surface proteins that is vital for infection, dissemination, and persistence. Here we characterized the expression pattern of bacterial surface antigens using different microscopy techniques, from fluorescent wide field to super-resolution and immunogold-scanning electron microscopy. A fluorescent strain ofB. burgdorferispirochetes was labeled with monoclonal antibodies directed against various bacterial surface antigens. Our results indicate that OspA is more evenly distributed over the surface than OspB and OspC that were present as punctate areas.

Crossed Immunoelectrophoresis In The Identification Of Platelet Membrane Glycoproteins And Complexes

1981 ◽  
Author(s):  
S Karpatkin ◽  
S Shulman ◽  
L Howard ◽  
S Sadanandan
Keyword(s):  
Concanavalin A ◽  
Surface Antigens ◽  
Platelet Membrane ◽  
Surface Proteins ◽  
Membrane Glycoproteins ◽  
Glanzmann’S Thrombasthenia ◽  
Crossed Immunoelectrophoresis ◽  
Platelet Membranes ◽  
Glanzmann's Thrombasthenia ◽  
Major Antigen

Human platelet membranes were solubilized in 1% Triton X-100 and subjected to crossed immunoelectrophoresis, employing a rabbit anti-piatelet membrane antibody. Ten different antigens were observed fairly consistently; one could be identified as albumin, the other as fibrinogen. Surface antigens were determined by antibody adsorbtion experiments, and cell surface labeling with 125I-lactoperoxidase. Four surface antigens reacted with concanavalin A, when this was employed as an intermediate spacer gel. A major surface antigen, 10, was present on all preparations and was inversely related to antigens 13 and 18, which moved more cathodally. Membranes from preparations with full 10 antigen peaks had absent or diminished 13 and 18 antigen peaks, whereas preparations with absent to incomplete cathodal curves had increased 13 and 18 antigen peaks. Digestion of intact washed platelets with α chymotrypsin resulted in a decrease in the 10 antigen peak and an increase in 13 and 18, suggesting a structural relationship. Extraction of platelet membranes in EDTA or EGTA resulted in the disappearance of 10 and appearance of 13 and 18 (which react with concanavalin A) and 15 and 16 (which do not). Splitting of the major antigen into 13, 18, 15 and 16 could be prevented by addition of excess Ca++ relative to EGTA (but not by excess Mg++). Similar results were obtained in the absence of chelating agents following dialysis at 60-200 hrs against ‘Ca++-free’ buffer. Five patients with Glanzmann’s thrombasthenia have been studied. All k components of the major membrane antigen are missing. We conclude that the major antigen, 10, is composed of 2 glycoproteins, 13 and 18, and 2 other surface proteins, 15 and 16, which are held together by Ca++. It is conceivable that patients with Glanzmann’s thrombasthenia are lacking a membrane receptor for Ca++ or the platelet membrane (glyco)protein which anchors these A components.

scholarly journals The crystal structure and localization of Trypanosoma brucei invariant surface glycoproteins suggest a more permissive VSG coat in the tsetse-transmitted metacyclic stage

2018 ◽  
Author(s):  
Aitor Casas-Sánchez ◽  
Samïrah Perally ◽  
Raghavendran Ramaswamy ◽  
Lee R. Haines ◽  
Clair Rose ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Trypanosoma Brucei ◽  
Fluorescent Microscopy ◽  
Surface Antigens ◽  
Surface Proteins ◽  
Surface Glycoprotein ◽  
Invariant Surface ◽  
Helical Bundle ◽  
N Terminus ◽  
Key Features

AbstractTrypanosoma brucei spp. develop into mammalian-infectious metacyclic trypomastigotes inside the tsetse salivary glands. Besides acquiring a variant surface glycoprotein (VSG) coat, nothing is known about expression of invariant surface antigens by the metacyclic stage. Proteomic analysis of saliva from T. brucei-infected flies revealed a novel family of hypothetical GPI-anchored surface proteins herein named Metacyclic Invariant Surface Proteins (MISP). MISP are encoded by five homolog genes and share ~80% protein identity. The crystal structure of MISP N-terminus at 1.82 Å resolution revealed a triple helical bundle that shares key features with other trypanosome surface proteins. However, molecular modelling combined with live fluorescent microscopy suggest that MISP N-termini are extended above the metacyclic VSG coat, exposing immunogenic epitopes. Collectively, we suggest that the metacyclic cell surface architecture appears more permissive than bloodstream forms in terms of expression of invariant GPI-anchored glycoproteins, which could be exploited for the development of novel vaccines against African trypanosomiases.

scholarly journals Antigenicity of the surface proteins of non o1 non o139 vibrio cholerae in rabbit model

1970 ◽  
Vol 19 (2) ◽  
pp. 129-135
Author(s):  
Tania S Bonny ◽  
Fazle Rabbi ◽  
Mahmuda Yasmin ◽  
Jamalun Nessa ◽  
Chowdhury R Ahsan
Keyword(s):  
Rabbit Model ◽  
Surface Antigens ◽  
Immunoblot Analysis ◽  
Surface Proteins ◽  
Diagnostic Tools ◽  
Coomassie Brilliant Blue ◽  
Antigenic Proteins ◽  
Sds Page ◽  
Antibody Titers ◽  
Coomassie Brilliant

An investigation was carried out to demonstrate the antigenicity of the surface proteins of the non O1 non O139 V. cholerae in rabbit model. Three rabbits were immunized with the surface proteins and sera were collected at one week intervals for six weeks. Sera were examined for antibodies specific for surface antigens using ELISA and the results showed a significant increase in antibody titers with time. The SDS?PAGE analysis showed a number of protein bands ranging from 21 to 131 kDa after Coomassie brilliant blue R250 staining. However, immunoblot analysis showed four major antigenic bands of 38, 43, 74 and 85 kDa to be prominent. These identified proteins might have higher immunogenic effects among humans infected with non O1 non O139 V. cholerae and some of these antigenic proteins could be included as diagnostic tools based on serology and also in vaccine preparations. Key words: Antigenicity; Surface proteins; Non O1 non O139 V. cholerae; Rabbit model DOI: http://dx.doi.org/10.3329/dujbs.v19i2.8954 DUJBS 2010; 19(2): 129-135

Allelic antigen and membrane-anchor epitopes of Paramecium primaurelia surface antigens

1987 ◽  
Vol 88 (5) ◽  
pp. 553-562
Author(s):  
YVONNE CAPDEVILLE ◽  
FRANCOIS CARON ◽  
CLAUDE ANTONY ◽  
CHRISTIANE DEREGNAUCOURT ◽  
ANNE-MARIE KELLER
Keyword(s):  
Surface Antigens ◽  
Immunogold Labelling ◽  
Polyclonal Antiserum ◽  
Surface Proteins ◽  
Soluble Form ◽  
Membrane Anchor ◽  
Membrane Bound ◽  
The Cross

Paramecium aurelia can express a repertoire of surface antigens (SAgs) according to culture conditions. These high Mr proteins are anchored in the plasma membrane by a glycolipid, and they can be isolated in two different forms, an amphiphilic membrane-bound form (mSAg) and a hydrophilic soluble form (sSAg). Endogenous or exogenous phospholipase C can convert mSAg to sSAg with unmasking of a carbohydrate antigenic determinant similar to that found in the soluble form of Trypanosoma variant surface glycoproteins and called the cross-reacting determinant. By immunizing mice with cilia from strain 156 of P. primaurelia expressing the G SAg, we obtained six monoclonal antibodies against the 156G SAg, which could be classified into two groups. Y4 and Y8, representative of each group, have been characterized by checking their reactivity in situ and in vivo towards a series of allelic G and D SAgs in P. primaurelia and the 51B SAg in P. tetraurelia. The monoclonal Y4 recognizes a conformational determinant, accessible in vivo and common to all the G SAgs. Thus, Y4 defines a G locus-specific epitope that corresponds to a conserved region inside a polymorphic domain. The monoclonal Y8 recognizes two homologous determinants whose detection depends on the presence or absence of the SAg membrane-anchor, and which are mutually exclusive: one is found in the reduced soluble form of all the SAgs and other surface proteins, the cross-reacting glycoproteins (CRGs); the other occurs in the unreduced membrane-bound form of the G SAgs. Thus, Y8 enables us to demonstrate that the membrane-anchor of Paramecium SAgs contains an additional hidden determinant close to the cross-reacting determinant and to discriminate between the membrane-bound and soluble form of SAgs. The in situ organization of the 156G SAg molecules is also discussed on the basis of immunogold labelling obtained using Y4 and a polyclonal antiserum.

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