scholarly journals The O Antigen Enables Bordetella parapertussis To Avoid Bordetella pertussis-Induced Immunity

2007 ◽  
Vol 75 (10) ◽  
pp. 4972-4979 ◽  
Author(s):  
Daniel N. Wolfe ◽  
Elizabeth M. Goebel ◽  
Ottar N. Bjornstad ◽  
Olivier Restif ◽  
Eric T. Harvill

ABSTRACT Bordetella pertussis and Bordetella parapertussis are closely related endemic human pathogens which cause whooping cough, a disease that is reemerging in human populations. Despite how closely related these pathogens are, their coexistence and the limited efficacy of B. pertussis vaccines against B. parapertussis suggest a lack of cross-protective immunity between the two. We sought to address the ability of infection-induced immunity against one of these pathogens to protect against subsequent infection by the other using a mouse model of infection. Immunity induced by B. parapertussis infection protected against subsequent infections by either species. However, immunity induced by B. pertussis infection prevented subsequent B. pertussis infections but did not protect against B. parapertussis infections. The O antigen of B. parapertussis inhibited binding of antibodies to the bacterial surface and was required for B. parapertussis to colonize mice convalescent from B. pertussis infection. Thus, the O antigen of B. parapertussis confers asymmetrical cross-immunity between the causative agents of whooping cough. We propose that these findings warrant investigation of the relative role of B. parapertussis in the resurgence of whooping cough.

2012 ◽  
Vol 80 (12) ◽  
pp. 4309-4316 ◽  
Author(s):  
Juan Gorgojo ◽  
Yanina Lamberti ◽  
Hugo Valdez ◽  
Eric T. Harvill ◽  
Maria Eugenia Rodríguez

ABSTRACTWhooping cough is a reemerging disease caused by two closely related pathogens,Bordetella pertussisandBordetella parapertussis. The incidence ofB. parapertussisin whooping cough cases has been increasing since the introduction of acellular pertussis vaccines containing purified antigens that are common to both strains. Recently published results demonstrated that these vaccines do not protect againstB. parapertussisdue to the presence of the O antigen on the bacterial surface that impairs antibody access to shared antigens. We have investigated the effect of the lack of opsonization ofB. parapertussison the outcome of its interaction with human neutrophils (polymorphonuclear leukocytes [PMNs]). In the absence of opsonic antibodies, PMN interaction withB. parapertussisresulted in nonbactericidal trafficking upon phagocytosis. A high percentage of nonopsonizedB. parapertussiswas found in nonacidic lysosome marker (lysosome-associated membrane protein [LAMP])-negative phagosomes with access to the host cell-recycling pathway of external nutrients, allowing bacterial survival as determined by intracellular CFU counts. The lipopolysaccharide (LPS) O antigen was found to be involved in directingB. parapertussisto PMN lipid rafts, eventually determining the nonbactericidal fate inside the PMN. IgG opsonization ofB. parapertussisdrastically changed this interaction by not only inducing efficient PMN phagocytosis but also promoting PMN bacterial killing. These data provide new insights into the immune mechanisms of hosts againstB. parapertussisand document the crucial importance of opsonic antibodies in immunity to this pathogen.


1962 ◽  
Vol 60 (3) ◽  
pp. 289-293 ◽  
Author(s):  
Neda Köhler-Kubelka

Investigations carried out to ascertain the ability of various strains of Bordetella pertussis and B. parapertussis to produce agglutinins have shown that the agglutinin response is considerably greater with B. parapertussis.Children inoculated with a combined vaccine in which the parapertussis element contained B. parapertussis in only one-twelfth of the concentration of B. pertussis in the pertussis element showed agglutinins in their sera in titres well above 1:300 for both organisms. There were no cross-reactions and the serological responses were specific throughout. The vaccine used was the standard diphtheria-tetanus-pertussis (DTP) prophylactic to which had been added a vaccine prepared from recently isolated strains of B. parapertussis.Agglutinin titres of both whooping cough components with the combined vaccine were somewhat lower in mice than was the case when monovalent vaccines were used, but they were considered to be satisfactory.It is suggested that the agglutination production test in mice could be used for the assessment of protective power of B. parapertussis vaccines against infection.I wish to thank Dr Ikić, director of the Institute of Immunology, Zagreb, who enabled me to perform all these examinations, further to Dr B. Mravunac and Dr Z. Radanov for having carried out vaccination in children and for the clinical examination of post vaccination reactions.


2015 ◽  
Vol 143 (12) ◽  
pp. 2619-2623 ◽  
Author(s):  
S. JAVED ◽  
F. SAID ◽  
S. A. M. A. S. EQANI ◽  
H. BOKHARI

SUMMARYPertussis or whooping cough is a highly contagious community disease mainly caused by Bordetella pertussis and B. parapertussis. We report a minor outbreak of whooping cough (2009–2010) in symptomatic subjects from Bisham, near Swat, Khyber Pukhtoonkhawa province, Pakistan. Interestingly, our results show that all the culture-positive isolates (n = 21) collected from children (average age 3·46 years), were identified as B. parapertussis after routine identification tests and PCR IS481, IS1001 and IS1002. Furthermore, in the affected patients, none had received immunization with diphtheria-pertussis-tetanus (DTPw) vaccine. Therefore, the possibility of the re-emergence of the disease due to limitation of basic health services as a result of the political unrest due to the 9/11 situation is also examined. Moreover, we discuss the importance of vaccinating both adults and children with DTPwPaw vaccine containing both organisms for better protection.


2014 ◽  
Vol 82 (12) ◽  
pp. 5175-5184 ◽  
Author(s):  
Juan Gorgojo ◽  
Eric T. Harvill ◽  
Maria Eugenia Rodríguez

ABSTRACTBordetella parapertussisis a human pathogen that causes whooping cough. The increasing incidence ofB. parapertussishas been attributed to the lack of cross protection induced by pertussis vaccines. It was previously shown thatB. parapertussisis able to avoid bacterial killing by polymorphonuclear leukocytes (PMN) if specific opsonic antibodies are not present at the site of interaction. Here, we evaluated the outcome ofB. parapertussisinnate interaction with human macrophages, a less aggressive type of cell and a known reservoir of many persistent pathogens. The results showed that in the absence of opsonins, O antigen allowsB. parapertussisto inhibit phagolysosomal fusion and to remain alive inside macrophages. The O antigen targetsB. parapertussisto lipid rafts that are retained in the membrane of phagosomes that do not undergo lysosomal maturation. Forty-eight hours after infection, wild-typeB. parapertussisbacteria but not the O antigen-deficient mutants were found colocalizing with lipid rafts and alive in nonacidic compartments. Taken together, our data suggest that in the absence of opsonic antibodies,B. parapertussissurvives inside macrophages by preventing phagolysosomal maturation in a lipid raft- and O antigen-dependent manner. Two days after infection, about 15% of macrophages were found loaded with live bacteria inside flotillin-enriched phagosomes that had access to nutrients provided by the host cell recycling pathway, suggesting the development of an intracellular infection. IgG opsonization drastically changed this interaction, inducing efficient bacterial killing. These results highlight the need forB. parapertussisopsonic antibodies to induce bacterial clearance and prevent the eventual establishment of cellular reservoirs of this pathogen.


Microbiology ◽  
2014 ◽  
Vol 160 (5) ◽  
pp. 962-969 ◽  
Author(s):  
N. Hegerle ◽  
N. Guiso

Whooping cough is a vaccine-preventable disease presenting with epidemic cycles linked to natural and/or vaccine-driven evolution of the aetiological agent of the disease, Bordetella pertussis. Adenylate cyclase–haemolysin (AC-Hly) is a major toxin produced by this pathogen, which mediates macrophage apoptosis in vitro and in vivo. While current acellular pertussis vaccine (APV) formulations do not include AC-Hly, they all contain pertussis toxin and can comprise filamentous haemagglutinin (FHA), which interacts with AC-Hly, and pertactin (PRN), which has been hypothesized also to interact with AC-Hly. We aimed to study the capacity of specific antibodies to inhibit the in vitro B. pertussis AC-Hly-mediated cytotoxicity of J774A.1 murine macrophages in a background of a changing bacterial population. We demonstrate that: (i) clinical isolates of different types or PRN phenotype are all cytotoxic and lethal in the mouse model of respiratory infection; (ii) lack of PRN production does not impact AC-Hly-related phenotypes; (iii) anti-AC-Hly antibodies inhibit cell lysis whatever the phenotype of the isolate, while anti-PRN antibodies significantly inhibit cell lysis provided the isolate produces this antigen, which might be relevant in vivo for APV-induced immunity; and (iv) anti-FHA antibodies only inhibit lysis induced by isolates collected in 2012, maybe indicating specific characteristics of epidemic lineages of B. pertussis.


2011 ◽  
Vol 43 (10) ◽  
pp. 818-820 ◽  
Author(s):  
Habib Bokhari ◽  
Fahad Said ◽  
Muhammad A. Syed ◽  
Amjad Mughal ◽  
Yasmeen F. Kazi ◽  
...  

1994 ◽  
Vol 180 (4) ◽  
pp. 1225-1233 ◽  
Author(s):  
Y Ishibashi ◽  
S Claus ◽  
D A Relman

Bordetella pertussis, the causative agent of whooping cough, adheres to human monocytes/macrophages by means of a bacterial surface-associated protein, filamentous hemagglutinin (FHA) and the leukocyte integrin, complement receptor 3 (CR3, alpha M beta 2, CD11b/CD18). We show that an FHA Arg-Gly-Asp site induces enhanced B. pertussis binding to monocytes, and that this enhancement is blocked by antibodies directed against CR3. Enhancement requires a monocyte signal transduction complex, composed of leukocyte response integrin (alpha? beta 3) and integrin-associated protein (CD47). This complex is known to upregulate CR3 binding activity. Thus, a bacterial pathogen enhances its own attachment to host cells by coopting a host cell signaling pathway.


2005 ◽  
Vol 73 (7) ◽  
pp. 4295-4301 ◽  
Author(s):  
Sylvie Alonso ◽  
Eve Willery ◽  
Genevieve Renauld-Mongénie ◽  
Camille Locht

ABSTRACT Bordetella pertussis, the etiologic agent of whooping cough, is a highly infectious human pathogen capable of inducing mucosal and systemic immune responses upon a single intranasal administration. In an attenuated, pertussis toxin (PTX)-deficient recombinant form, it may therefore constitute an efficient bacterial vector that is particularly well adapted for the delivery of heterologous antigens to the respiratory mucosa. Filamentous hemagglutinin (FHA) has been used as a carrier to present foreign antigens at the bacterial surface, thereby inducing local, systemic, and protective immune responses to these antigens in mice. Both full-length and truncated (Fha44) forms of FHA have been used for antigen presentation. To investigate the effect of the carrier (FHA or Fha44) on antibody responses to passenger antigens, we genetically fused the HtrA protein of nontypeable Haemophilus influenzae to either FHA form. The fha-htrA and Fha44 gene-htrA hybrids were expressed as single copies inserted into the chromosome of PTX-deficient B. pertussis. Both chimeras were secreted into the culture supernatants of the recombinant strains and were recognized by anti-FHA and anti-HtrA antibodies. Intranasal infection with the strain producing the FHA-HtrA hybrid led to significantly higher anti-HtrA and anti-FHA antibody titers than those obtained in mice infected with the Fha44-HtrA-producing strain. Interestingly, the B. pertussis strain producing the Fha44-HtrA chimera colonized the mouse lungs more efficiently than the parental, Fha44-producing strain and gave rise to higher anti-FHA antibody titers than those induced by the parental strain.


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