Immunoglobulin G binding proteins in male <i>Rhipicephalus appendiculatus</i> ticks

Wang, Hui; Nuttall, Patricia A.

doi:10.1111/j.1365-3024.1995.tb00882.x

Cited by 30 publications

(24 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The ability of antibody to fix complement may explain the differential effects of natural IgM and IgG in these assays. In addition, tick saliva contains IgG binding proteins that can sequester IgG, possibly to prevent damage to the tick, and spirochetes may indirectly benefit from this tick defense mechanism (40). IgM may exert selective pressure on spirochetes such that those with reduced levels of surface-exposed Osps, including OspA, have much higher survival rates.…”

Section: Discussionmentioning

confidence: 99%

Natural Antibody Affects Survival of the SpirocheteBorrelia burgdorferiwithin Feeding Ticks

Belperron

2001

Infect Immun

View full text Add to dashboard Cite

Natural antibodies are those immunoglobulin molecules found in mammalian serum that arise in the absence of exposure to environmental pathogens and may comprise an early host defense against invading pathogens. The spirochete Borrelia burgdorferi first encounters natural antibodies when its arthropod vector, Ixodes scapularis, begins feeding on a mammalian host. Natural antibodies may therefore have an impact on pathogens within blood-sucking vectors, prior to pathogen transmission to the mammal. In this study, we investigated whether natural antibodies influenced the number and/or phenotype of B. burgdorferi organisms within feeding I. scapularis nymphs. Using a competitive PCR, we found that ticks ingesting a blood meal from B-cell-deficient mice, which lack all immunoglobulins, contained fivefold more spirochete DNA than ticks feeding on control mice. Spirochete DNA levels could be reduced to that of controls with passive transfer of normal mouse serum or polyclonal immunoglobulin M (IgM), but not IgG, into B-cell-deficient mice prior to placement of infected ticks. At 48 h of tick feeding, 90% of spirochetes within salivary glands of ticks removed from B-cell-deficient mice were found by confocal immunofluorescence microscopy to express outer surface protein A (OspA), compared to only 5% of salivary gland spirochetes from ticks detached from control mice. Taken together, these results show that ingestion of natural antibodies limits the spirochete burden within feeding ticks. Because OspA is normally downregulated when spirochetes moved from the tick midgut to the salivary gland, our findings suggest that OspA-expressing midgut spirochetes may be particularly susceptible to the borrelicidal effects of these molecules.

show abstract

Section: Discussionmentioning

confidence: 99%

Natural Antibody Affects Survival of the SpirocheteBorrelia burgdorferiwithin Feeding Ticks

Belperron

2001

Infect Immun

View full text Add to dashboard Cite

show abstract

“…Male R. appendiculatus ticks have a 54-kDa salivary gland IGBP similar to that of the females. However, unlike the female IGBP that binds IgGs from guinea pig, human and bovine hosts, the male 54-kDa IGBP does not bind to bovine IgG [51]. This variation in IgG-binding host specificity suggests that the IgG-excreting mechanism may differ between conspecific male and female ticks.…”

Section: Male Igbps In R Appendiculatusmentioning

confidence: 69%

“…Indeed, the 54-kDa IGBP is not the most abundant IGBP in the male salivary glands, whereas it is the major IGBP band in the female SGE. Three more abundant IGBPs are present in the partially fed male SGE [51]. The 21-kDa band, designated IGBPMC, bound to IgG of three potential host species (guinea pig, human and bovine), whereas the 29-kDa IGBPMA did not bind to bovine IgG.…”

Section: Male Igbps In R Appendiculatusmentioning

confidence: 96%

“…These haemolymph IGBPs may carry out the function of IgG recognition, whereas the salivary gland IGBPs may be responsible for IgG excretion. The 54-kDa IGBP from female [50] and 21-kDa from male [51] SGEs of day 6-fed R. appendiculatus ticks were able to bind IgG of guinea pigs, on which host the tick colony was maintained, and also other mammalian IgGs tested (human and bovine). Although IGBPs vary in different tick species (at least in size), it appears that the general mechanism of clearing host IgG is widespread among ixodid ticks.…”

Section: H Wang and P A Nuttalmentioning

confidence: 96%

See 1 more Smart Citation

Immunoglobulin-binding proteins in ticks: new target for vaccine development against a blood-feeding parasite

Wang¹,

Nuttall²

1999

CMLS, Cell. Mol. Life Sci.

100

View full text Add to dashboard Cite

Humans have a long history of trying to control ticks. At first, attempts focused on modifying the habitat, whereas later efforts relied heavily on the use of chemicals. Current research is directed at finding a vaccine against ticks. A strategy of targeting 'concealed antigens' succeeded with the first commercialised vaccine against the cattle tick Boophilus microplus. However, vaccine development against other tick species appears unsatisfactory to date. Vaccination depends on a specific antibody-mediated immunoreaction that damages the parasite. Immunoglobulin molecules of vertebrate hosts can pass through gut barriers into the haemolymph of ectoparasites while retaining antibody activity. Research on the ixodid tick Rhipicephalus appendiculatus revealed that host immunoglobulin-G in the parasite was excreted via salivation, during feeding. Immunoglobulin-binding proteins in tick haemolymph and salivary glands are thought to be responsible for such excretion. The discovery of an immunoglobulin excretion system in ticks indicates that they have a highly developed mechanism to protect themselves from their host's antibody attack. Such a mechanism questions whether immunization strategies will be effective against ticks, unless they circumvent or disable the ticks' immunoglobulin excretion system.

show abstract

“…Salivary glands of R. appendiculatus male ticks contain a number of IgB proteins. It has been postulated that males secrete a cocktail of IgB proteins into the feeding lesion where they help protect adjacent females from the host's anti-tick immune response (Wang and Nuttall 1995b).…”

Section: Discussionmentioning

confidence: 99%

An Immunoglobulin Binding Protein (Antigen 5) of the Stable Fly (Diptera: Muscidae) Salivary Gland Stimulates Bovine Immune Responses

Ameri

Wang

Wilkerson

et al. 2008

Journal of Medical Entomology

View full text Add to dashboard Cite

The stable fly, Stomoxys calcitrans, is an economically important pest of livestock. Prior studies demonstrated lymphocyte suppression by crude salivary gland extract (SGE) of the stable fly. A dominant 27 kDa protein identified in the SGE was reported to stimulate immunodominant antibody responses in exposed cattle. The purpose of this study was to determine if this protein, now identified as a homolog of insect proteins named antigen 5 (Ag5), was responsible for the lymphocyte suppression and if naïve calves can mount an immune response to it. Calves raised in the winter months were immunized with recombinant Ag5 (rAg5) expressed in Drosophila S2 cells or with "natural" Ag5 protein isolated by preparative gel electrophoresis of SGE. Control calves were immunized with adjuvant alone. Rising antibody concentrations to rAg5 were detected in two of three calves immunized with rAg5 and one of three calves immunized with natural Ag5. Recall lymphocyte responses to rAg5 were detected at 21 and 28 DPI in calves immunized with rAg5 but not in calves immunized with the natural Ag5 or those exposed to adjuvant alone. Mitogen-stimulated bovine lymphocyte responses were not suppressed by rAg5. Further investigation using immunoblotting revealed that rAg5 binds to the Fc and F(ab') 2 portions of bovine IgG, but not to an Fab fragment. These findings suggest that Ag5 of the stable fly salivary gland is not immunosuppressive, but has immunoglobulin binding properties and can invoke specific antibody and memory lymphocyte responses in immunized calves.Keywords bovine lymphocytes; lymphocyte suppression; antibody; stable fly; salivary gland protein The stable fly, Stomoxys calcitrans (L.), is an economically important pest affecting the health of cattle in feedlots (Campbell et al. 1987) and dairies (Stork 1979). The latest estimate for economic loss to the U.S. livestock industry is $428 million/year (Kunz et al. 1991). Within the past decade several investigators have noted the stable fly has extended its pest distribution to range or pastured cattle (Campbell et al. 2001a, Campbell et al. 2001c. Studies indicate that the wasted hay/manure mixture at winter feeding sites of hay in round bales is the main source

show abstract

Immunoglobulin G binding proteins in male Rhipicephalus appendiculatus ticks

Cited by 30 publications

References 15 publications

Natural Antibody Affects Survival of the SpirocheteBorrelia burgdorferiwithin Feeding Ticks

Natural Antibody Affects Survival of the SpirocheteBorrelia burgdorferiwithin Feeding Ticks

Immunoglobulin-binding proteins in ticks: new target for vaccine development against a blood-feeding parasite

An Immunoglobulin Binding Protein (Antigen 5) of the Stable Fly (Diptera: Muscidae) Salivary Gland Stimulates Bovine Immune Responses

Contact Info

Product

Resources

About