Structural requirements for glycosaminoglycan recognition by the Lyme disease spirochete, Borrelia burgdorferi.

نویسندگان

  • J M Leong
  • D Robbins
  • L Rosenfeld
  • B Lahiri
  • N Parveen
چکیده

Borrelia burgdorferi, the Lyme disease agent, binds glycosaminoglycans (GAGs) such as heparin, heparan sulfate, and dermatan sulfate. Heparin or heparan sulfate fractions separated by size or charge were tested for their ability to inhibit attachment of B. burgdorferi to Vero cells. GAG chains of increasing length and/or charge showed increasing inhibitory potency, and detectable heparin inhibition of bacterial binding required a minimum of 16 residues. The ability of a given heparin fraction to inhibit binding to Vero cells was strongly predictive of its ability to inhibit hemagglutination, suggesting that hemagglutination reflects the capacity of B. burgdorferi to bind to GAGs.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Identification of Two Epitopes on the Outer Surface Protein A of the Lyme Disease Spirochete Borrelia burgdorferi

A murine IgM monoclonal antibody (MA-2C6) with κ-light chains directed against an antigenic determinant of outer surface protein A (OspA) of the Lyme disease spirochete, Borreliaburgdorferi, is produced. This antibody could bind specifically to OspA antigen of several isolates of B. burgdorferi, but not to the non-Lyme disease bacteria such as T. pallidum and B. hermsii. Antibody MA-2C6 was pur...

متن کامل

Report of a case of Lyme disease in Mazandaran

Lyme disease is caused by the spirochete Borrelia burgdorferi. Depending on the stage of illness, infection may be limited to the skin or involve the cardiac, nervous and musculoskeletal systems. Herein, we report a case of Lyme disease in a 23-year-old woman from North of Iran (Mazandaran) in early-localized stage of erythema chronicum migrans. The diagnosis was confirmed by the presence of se...

متن کامل

Hemagglutination and proteoglycan binding by the Lyme disease spirochete, Borrelia burgdorferi.

The ability of the Lyme disease spirochete to attach to host components may contribute to its ability to infect diverse tissues. We present evidence that the Lyme disease spirochete expresses a lectin activity that promotes agglutination of erythrocytes and bacterial attachment to glycosaminoglycans. Among a diverse collection of 21 strains of Lyme disease spirochete, hemagglutinating activity ...

متن کامل

Borrelia burgdorferi glycosaminoglycan-binding proteins: a potential target for new therapeutics against Lyme disease.

The spirochete bacterium Borrelia burgdorferi sensu lato is the causative agent of Lyme disease, the most common vector-borne disease in Europe and the United States. The spirochetes can be transmitted to humans via ticks, and then spread to different tissues, leading to arthritis, carditis and neuroborreliosis. Although antibiotics have commonly been used to treat infected individuals, some tr...

متن کامل

Tube phagocytosis, a novel way for neutrophils to Phagocytize borrelia burgdorferi.

Interactions between human neutrophils and Borrelia burgdorferi, the Lyme disease spirochete, were studied by dark-field microscopy combined with video technology. A previously unrecognized mechanism for neutrophils to phagocytize the spirochete was discovered. During phagocytosis, the spirochete attaches to the neutrophil head-on, the neutrophil forms a thin tubelike protrusion around the bact...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Infection and immunity

دوره 66 12  شماره 

صفحات  -

تاریخ انتشار 1998