Steric hindrance of antibody binding to surface proteins of Coxiella burnetti by phase I lipopolysaccharide

Hackstadt, Ted

doi:10.1128/iai.56.4.802-807.1988

Cited by 65 publications

(23 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Hindrance of antibody access has been noted in other pathogens. In gram-negative bacteria, such as Neisseria gonorrhoeae, E. coli, and Brucella spp., lipooligosaccharides or lipopolysaccharides shield porin proteins from antibody (21,29,60). B. burgdorferi lacks these molecules (59) but instead expresses abundant Osp proteins that appear to hinder the access to other outer membrane proteins.…”

Section: Discussionmentioning

confidence: 99%

Access of Antibody or Trypsin to an Integral Outer Membrane Protein (P66) ofBorrelia burgdorferiIs Hindered by Osp Lipoproteins

1999

View full text Add to dashboard Cite

The outer membrane of Borrelia burgdorferi, the Lyme disease agent, contains lipoproteins anchored by their lipid moieties and integral proteins with membrane-spanning regions. We used the techniques of in situ proteolysis, immunofluorescence, in vitro growth inhibition, and cross-linking with formaldehyde to characterize topological relationships between P66, an integral membrane protein, and selected Osp lipoproteins of B. burgdorferi. Protease treatment of intact spirochetes cleaved P66 and Osp proteins but not the periplasmic flagellin or the BmpA protein of the cytoplasmic membrane. P66 of cells lacking OspA, OspB, and OspC was more susceptible to trypsin cleavage than was P66 of cells with these Osp proteins. A monoclonal antibody against the surface loop of P66 bound, agglutinated, and inhibited the growth of viable spirochetes lacking OspA, OspB, OspC, and OspD but not of the cells that expressed OspA, OspC, and/or OspD. When cells were fixed, the antibody bound to cells that express OspD and OspC but still not to cells with OspA. The close association of OspA and P66 was confirmed by the crosslinking of the two proteins by formaldehyde. These results show that Osp proteins, particularly OspA, limit the access of antibody or trypsin to the surface loop region of P66. The proximity and possible contact between P66 and OspA (or other Osp proteins) may hinder the effectiveness of antibodies to what otherwise would be an appropriate vaccine target.

show abstract

Section: Discussionmentioning

confidence: 99%

Access of Antibody or Trypsin to an Integral Outer Membrane Protein (P66) ofBorrelia burgdorferiIs Hindered by Osp Lipoproteins

1999

View full text Add to dashboard Cite

show abstract

“…First, it has been shown that the Intracellular bacterium Coxiella burnetti undergoes a phase variation in which the highly virulent Phase I organism has very large amounts of LPS on its surface. Antibody raised against bacteria growing in the second (less virulent) phase cannot recognize proteins on the surface of the Phase I organism because of steric hindrance by LPS (Hackstadt, 1988). Inasmuch as antibody is able to recognize Jnvasin on the surface of Shigella.…”

Section: Discussionmentioning

confidence: 99%

An O antigen can interfere with the function of the Yersinia pseudotuberculosis invasin protein

Voorhis

Dillon

Formal

et al. 1991

Molecular Microbiology

View full text Add to dashboard Cite

Escherichia coli strains harbouring the Yersinia pseudotuberculosis inv gene are able to enter cultured mammalial cells. We show here that this property is not shared by all enteric bacteria, since Shigella flexneri 2a cured of its virulence-associated plasmid and harbouring the inv gene is unable to enter mammalian cells efficiently. Mapping studies showed that the region of the chromosome responsible for this phenotype includes rfaB, a locus involved in the production of O antigen. S. flexneri 2a strains that express O antigen were unable to enter mammalian cells, even though invasin was efficiently expressed and localized, showing that this structure interferes with invasin activity. The O antigen either masks invasin or sterically hinders the ability of the mammalian cell receptor to bind this protein.

show abstract

“…burnetii displays antigenic variations similar to the smooth-rough variation in the family Enterobacteriaceae. Phase variation is related mainly to mutational variation in the lipopolysaccharide (LPS) (129)(130)(131). Phase I is the natural phase found in infected animals, arthropods, or humans.…”

Section: Bacteriologymentioning

confidence: 99%

Q Fever

1999

View full text Add to dashboard Cite

SUMMARY Q fever is a zoonosis with a worldwide distribution with the exception of New Zealand. The disease is caused by Coxiella burnetii, a strictly intracellular, gram-negative bacterium. Many species of mammals, birds, and ticks are reservoirs of C. burnetii in nature. C. burnetii infection is most often latent in animals, with persistent shedding of bacteria into the environment. However, in females intermittent high-level shedding occurs at the time of parturition, with millions of bacteria being released per gram of placenta. Humans are usually infected by contaminated aerosols from domestic animals, particularly after contact with parturient females and their birth products. Although often asymptomatic, Q fever may manifest in humans as an acute disease (mainly as a self-limited febrile illness, pneumonia, or hepatitis) or as a chronic disease (mainly endocarditis), especially in patients with previous valvulopathy and to a lesser extent in immunocompromised hosts and in pregnant women. Specific diagnosis of Q fever remains based upon serology. Immunoglobulin M (IgM) and IgG antiphase II antibodies are detected 2 to 3 weeks after infection with C. burnetii, whereas the presence of IgG antiphase I C. burnetii antibodies at titers of ≥1:800 by microimmunofluorescence is indicative of chronic Q fever. The tetracyclines are still considered the mainstay of antibiotic therapy of acute Q fever, whereas antibiotic combinations administered over prolonged periods are necessary to prevent relapses in Q fever endocarditis patients. Although the protective role of Q fever vaccination with whole-cell extracts has been established, the population which should be primarily vaccinated remains to be clearly identified. Vaccination should probably be considered in the population at high risk for Q fever endocarditis.

show abstract

Steric hindrance of antibody binding to surface proteins of Coxiella burnetti by phase I lipopolysaccharide

Cited by 65 publications

References 29 publications

Access of Antibody or Trypsin to an Integral Outer Membrane Protein (P66) ofBorrelia burgdorferiIs Hindered by Osp Lipoproteins

Access of Antibody or Trypsin to an Integral Outer Membrane Protein (P66) ofBorrelia burgdorferiIs Hindered by Osp Lipoproteins

An O antigen can interfere with the function of the Yersinia pseudotuberculosis invasin protein

Q Fever

Contact Info

Product

Resources

About