Safety and immunogenicity of an outer surface protein A vaccine in subjects with previous Lyme disease.

The safety and immunogenicity of a recombinant outer surface protein A (OspA) Lyme vaccine in patients previously diagnosed with Lyme disease was assessed in a dose-ranging, prospective study. Thirty healthy volunteers were consecutively assigned to receive three doses of 3, 10, or 30 micrograms of OspA vaccine at 0, 1, and 2 months. Subjects were seen 3 days after each vaccine dose and 1 month after completion of the three-dose schedule. Local side effects included soreness, induration, swelling, and redness. Transient systemic side effects occurred in 21 subjects, the majority of which (81%) were characterized as mild. Solicited symptoms included migratory mild arthralgias that lasted 24 h in 3 subjects. Side effects were not more evident after the second or third dose. Of the patients, 93% developed high-titer OspA antibodies. Thus, an OspA vaccine may be safe and immunogenic in patients with a history of Lyme disease.

Evaluation of a Lyme disease enzyme immunoassay using the 41-G fragment of flagellin.

An immunogenic region of the Borrelia burgdorferi flagellin encompassing amino acids 197-273 and designated 41-G was evaluated as an antigen in an enzyme immunoassay (EIA) for Lyme disease on a routine basis in a reference laboratory. Sera that tested positive for Lyme disease by EIA using 41-G or the whole-cell Borrelia burgdorferi lysate as the antigen were also evaluated by immunoblot for reactivity with Borrelia burgdorferi, and the patient's clinical history was determined retrospectively by a questionnaire distributed to the referring physician. The sensitivity of the 41-G based EIA for the serologic diagnosis of Lyme disease, when compared with that of the Borrelia burgdorferi lysate EIA, was 70% (35 of 50). These data demonstrate that 41-G has utility as an antigen in EIA, although the sensitivity is at present less than that of the assay employing the Borrelia burgdorferi whole-cell lysate.

Cytokineplasts from human blood polymorphonuclear leukocytes. Lack of oxidase activity and extended functional longevity.

Cytokineplasts (CKPs) are membrane-bounded, anucleate, granule-poor cytoplasmic fragments, induced from PMNs by brief heat (45 degrees C, 9 min), which retain motile function including chemotaxis and phagocytosis. CKPs can respond to repeated chemotactic stimuli even after having been held overnight at room temperature, and hence "outlive" control PMNs. We now report that adherent CKPs lack significant oxidase activity, as measured by reduction of nitroblue tetrazolium (NBT) dye, (1) 5 min after heat, when they are often still attached to their parent PMNs (which generally do not reduce NBT either); (2) later on, when they are free; and (3) when cells have been pretreated on endotoxin-coated substrata or with phorbol myristate acetate (PMA); both pretreatments cause the large majority of adherent control PMNs to reduce NBT. Moreover, cells harvested from glass just after heat lack the normal increase in oxygen consumption seen on stimulation with PMA or with heat-killed staphylococci. PMA-stimulated respiratory burst activity was not restored to heated cells by exogenous NADPH. Thus, heat applied to normal PMNs can dissociate motile function from oxidase activity; in this respect CKPs resemble PMNs in chronic granulomatous disease. The apparent increased functional stability of CKPs may indicate that normal PMNs are not immune to their own oxidative killing mechanism.