scholarly journals Citrus microcarpa Extract as Immunostimulator in Controlling Edwardsiellosis in African Catfish Culture

2015 ◽  
Vol 2 (2) ◽  
pp. 68-71
Author(s):  
Seong Wei Lee ◽  
MN An’amt ◽  
Wee Wendy ◽  
A.K. Zulhisyam

This study was described Citrus microcarpa extract as an antimicrobial agent in controlling edwardsiellosis in African catfish culture. Edwardsiellosis due to Edwardsiella tarda was recognized as a problem in African catfish culture and may lead to mass mortality of the cultured fish. Many antibiotics were no longer effective to control this bacterial disease. Therefore, this study was carried out to investigate the potential of C. microcarpa extract to overcome this bacterial disease problem. The experimental fish were fed with medicated feed at three different concentrations (1 g kg-1; CM-1, 2 g kg-1; CM-2 and 4 g kg-1 of fish) of C. microcarpa extract for one week before they were intraperitoneally exposed to E. tarda. Enzyme linked immunosorbent assay (ELISA) was carried out to determine the value of antibody response to E. tarda in fish from group of fish that received medicated fish and the percentage of total cumulative mortality of the experimental fish were observed at the end of the experiment. The results showed that the value of antibody response to E. tarda in fish from group of fish which received medicated feed (CM-1, 0.148 ± 0.017 OD; CM-2, 0.143 ± 0.006 OD; CM-4, 0.163 ± 0.015 OD) were found significantly higher (P < 0.05) compared to fish did not received medicated fish (0.00 OD). Whereas, percentage cumulative mortality of fish from all groups of fish received medicated feed (CM-1, 20.0 ± 10.0 %; CM-2, 16.7 ± 5.8 %; CM-4, 16.7 ± 5.8 %) were found significantly lower (P < 0.05) compared to group of fish did not received medicated feed (56.7 ± 5.8 %). The findings of the present study indicated the huge potential of C. microcarpa extract as natural antimicrobial agent for aquaculture use.

2021 ◽  
Vol 6 (1) ◽  
pp. 19-22
Author(s):  
Zulhisyam Abdul Kari ◽  
Wendy Wee ◽  
Lee Seong Wei

This paper described the application of Citrus microcarpa extract as bio-immunostimulator in red hybrid tilapia against Edwardsiellosis infection. Edwardsiellosis due to Edwardsiella tarda is one of the well-known bacterial diseases in aquaculture which leads to significant economic losses. The increasing antibiotic resistant cases among pathogenic bacteria led to many commercial antibiotics no longer effective in controlling bacterial diseases in aquaculture. Hence, in the present study was carried out to evaluate potential of C. microcarpa extract as immunostimulator against Edwardsiellosis infection in red hybrid tilapia. Comparison in terms of cumulative mortalities and antibody response against E. tarda among group of fish received C. microcarpa extract at different concentrations (CM1-1, 1 g kg-1 of fish; CM-2, 2 g kg-1 of fish and CM-4, 4 g kg-1 of fish) and group of fish received no medicated commercial feed (control) was carried out in the present study. Enzyme linked immunosorbent assay (ELISA) was used to monitor antibody response of fish that received medicated feed. The results of the present study showed that the values of antibody response against E. tarda of fish after seven days received C. microcarpa extract (CM-1, 0.113 ± 0.02 OD; CM-2, 0.14 ± 0.02 OD; CM-4, 0.173 ± 0.03 OD) were significantly higher (P < 0.05) compared to fish from group of control (0.0 OD). Whereas cumulative mortality of fish from group of control (53.3 ± 11.5 %) was significantly higher (P < 0.05) compared to fish from all of groups received C. microcarpa extract (CM-1, 13.3 ± 5.8 %; CM-2, 13.3 ± 5.8 % and CM-4, 6.7 ± 5.8 %). The results indicated the potential of C. microcarpa extract as immunostimulator in finfish culture.


2001 ◽  
Vol 69 (5) ◽  
pp. 3224-3231 ◽  
Author(s):  
Fang Ting Liang ◽  
Lisa C. Bowers ◽  
Mario T. Philipp

ABSTRACT VlsE, the variable surface antigen of Borrelia burgdorferi, contains two invariable domains located at the amino and carboxyl terminal ends, respectively, and a central variable domain. In this study, both immunogenicity and antigenic conservation of the C-terminal invariable domain were assessed. Mouse antiserum to a 51-mer synthetic peptide (Ct) which reproduced the entire sequence of the C-terminal invariable domain of VlsE from B. burgdorferi strain B31 was reacted on immunoblots with whole-cell lysates extracted from spirochetes of 12 strains from the B. burgdorferi sensu lato species complex. The antiserum recognized only VlsE from strain B31, indicating that epitopes of this domain differed among these strains. When Ct was used as enzyme-linked immunosorbent assay (ELISA) antigen, all of the seven monkeys and six mice that were infected with B31 spirochetes produced a strong antibody response to this peptide, indicating that the C-terminal invariable domain is immunodominant. None of 12 monkeys and only 11 of 26 mice that were infected with strains other than B31 produced a detectable anti-Ct response, indicating a limited antigenic conservation of this domain among these strains. Twenty-six of 33 dogs that were experimentally infected by tick inoculation were positive by the Ct ELISA, while only 5 of 18 serum samples from dogs clinically diagnosed with Lyme disease contained detectable anti-Ct antibody. Fifty-seven of 64 serum specimens that were collected from American patients with Lyme disease were positive by the Ct ELISA, while only 12 of 21 European samples contained detectable anti-Ct antibody. In contrast, antibody to the more conserved invariable region IR6 of VlsE was present in all of these dog and human serum samples.


mSphere ◽  
2018 ◽  
Vol 3 (2) ◽  
pp. e00590-17
Author(s):  
P. Martijn den Reijer ◽  
Mehri Tavakol ◽  
Nicole Lemmens-den Toom ◽  
Dikra Allouch ◽  
Sheila Thomas ◽  
...  

ABSTRACTThe fibronectin-binding protein A (FnBPA) is a cell surface-associated protein ofStaphylococcus aureuswhich mediates adherence to the host extracellular matrix and is important for bacterial virulence. Previously, substantial sequence diversity was found among strains in the fibrinogen-binding A domain of this protein, and 7 different isotypes were described. The effect of this sequence diversity on the human antibody response, in terms of both antibody production and antibody function, remains unclear. In this study, we identify five different FnBPA A domain isotypes based on the sequence results of 22 clinicalS. aureusisolates, obtained from the same number of patients suffering from bacteremia. Using a bead-based Luminex technique, we measure the patients’ total immunoglobulin G (IgG) against the 7 FnBPA isotypes at the onset and during the time course of bacteremia (median of 10 serum samples per patient over a median of 35 days). A significant increase in IgG against the FnBPA A domain, including the isotype carried by the infecting strain, is observed in only three out of 22 patients (14%) after the onset of bacteremia. Using a Luminex-based FnBPA–fibrinogen-binding assay, we find that preincubation of recombinant FnBPA isotypes with IgG from diverse patients does not interfere with binding to fibrinogen. This observation is confirmed using an alternative Luminex-based assay and enzyme-linked immunosorbent assay (ELISA).IMPORTANCEDespite the manyin vitroand murinein vivostudies involving FnBPA, the actual presence of this virulence factor during human infection is less well established. Furthermore, it is currently unknown to what extent sequence variation in such a virulence factor affects the human antibody response and the ability of antibodies to interfere with FnBPA function. This study sheds new light on these issues. First, the uniform presence of a patient’s IgG against FnBPA indicates the presence and importance of this virulence factor duringS. aureuspathogenesis. Second, the absence of an increase in antibody production in most patients following bacteremia indicates the complexity ofS. aureus-host interactions, possibly involving immune evasion or lack of expression of FnBPA during invasive infection. Finally, we provide new insights into the inability of human antibodies to interfere with FnBPA-fibrinogen binding. These observations should be taken into account during the development of novel vaccination approaches.


2009 ◽  
Vol 57 (13) ◽  
pp. 5687-5692 ◽  
Author(s):  
Chu-Chen Cheng ◽  
Kuan-Huei Hsieh ◽  
Yi-Chih Lei ◽  
Yung-Te Tai ◽  
Tong-Hsuan Chang ◽  
...  

2014 ◽  
Vol 12 (1) ◽  
pp. 75-79 ◽  
Author(s):  
Kamel Alhanout ◽  
Carole D. Giorgio ◽  
Michel D. Meo ◽  
Jean M. Brunel

2015 ◽  
Vol 23 (3) ◽  
pp. 141-148 ◽  
Author(s):  
Thangapalam Jawahar Abraham ◽  
Prakash Kumar Mallick ◽  
Harresh Adikesavalu ◽  
Sayani Banerjee

AbstractEdwardsiella tarda is one of the serious fish pathogens infecting both cultured and wild fish species. This study aimed to assess the phenotypic characterization and pathogenicity of E. tarda isolated from Clarias gariepinus (Burchell) with dropsy and histopathological alterations. The causative agent was identified with Vitek 2, and its pathogenicity was determined by intramuscular injection. The challenged catfish exhibited vertical hanging, frothing, excess mucus production, listing, swollen abdomen, anorexia, fin and tail rot, and reddish operculum. The LD50of E. tarda PBB and PBP strains was found to be 8.52 × 106and 1.68 × 107cells fish-1, respectively. Histopathological observations on catfish infected naturally revealed lymphocyte infiltration in muscle and focal necrosis, hyperplasia, edema, and swelling of the gill lamellar epithelium. The kidney of diseased fish exhibited ischemic type tubulopathy, necrosis of nephritic tubules, hyperplastic hematopoietic tissue, rupture of the tubular basement membrane, hydropic dystrophy of nephritic cells, neutrophil infiltration, fibrinoid necrosis of nephretic tubules, hemosiderin deposition, and edema. The liver sections revealed lymphocyte infiltration, dilation of hepatic sinusoids, expansion of space between hepatic sinusoids, and focal necrosis. The inflammatory responses observed in kidney and liver in the present study were presumably suppuration and were attributed to the potential virulence factors of E. tarda.


Author(s):  
Zofia Nuc ◽  
◽  
Aldona Dobrzycka-Krahel

Chitin is a naturally occurring polymer. Together with its derivatives such as chitosan, it has a wide spectrum of application possibilities, and many properties not yet exploited. Chitosan possesses many features desirable in an ideal antimicrobial polymer. It shows activity against multidrug-resistant bacterial and fungal strains that pose a challenge to modern medicine. Chitosan also shows activity against certain viruses, such as SARS-CoV-2. It might be used as a drug or a vaccine delivery system, is biodegradable, bioavailable and considered safe for medical use. It is important to continue exploring the potential of chitosan, as well as to investigate its sources. Indeed, many sources of this polymer are still not or have been poorly described. In this paper, we compile the current state of knowledge on the antimicrobial properties of chitosan, list alternative sources of chitin to highlight the potential of these two polymers and encourage further research.


2001 ◽  
Vol 69 (2) ◽  
pp. 1009-1015 ◽  
Author(s):  
Alan G. Barbour ◽  
Virgilio Bundoc

ABSTRACT The antigenic variation of the relapsing fever agent Borrelia hermsii is associated with changes in the expression of the Vlp and Vsp outer membrane lipoproteins. To investigate whether these serotype-defining proteins are the target of a neutralizing and protective antibody response, monoclonal antibodies were produced from spleens of infected mice just after clearance of serotype 7 cells from the blood. Two immunoglobulin M monoclonal antibodies, H7-7 and H7-12, were studied in detail. Both antibodies specifically agglutinated serotype 7 cells and inhibited their growth in vitro. Administered to mice before or after infection, both antibodies provided protection against infection or substantially reduced the number of spirochetes in the blood of mice after infection. Whereas antibody H7-12 bound to Vlp7 in Western blotting, enzyme-linked immunosorbent assay, and immunoprecipitation assays, as well as to whole cells in other immunoassays, antibody H7-7 only bound to wet, intact cells of serotype 7. Antibody H7-7 selected against cells expressing Vlp7 in vitro and in vivo, an indication that Vlp7 was a conformation-sensitive antigen for the antibody. Vaccination of mice with recombinant Vlp7 with adjuvant elicited antibodies that bound to fixed whole cells of serotype 7 and to Vlp7 in Western blots, but these antibodies did not inhibit the growth of serotype 7 in vitro and did not provide protection against an infectious challenge with serotype 7. The study established that a Vlp protein was the target of a neutralizing antibody response, and it also indicated that the conformation and/or the native topology of Vlp were important for eliciting that immunity.


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