Immunization of bovines with an aspartic proteinase precursor isolated from Boophilus microplus eggs

Vaz, Itabajara da Silva; Logullod, Carlos; Sorgine, Marcos Henrique Ferreira; Velloso, Fernando F.; Lima, Monica Fernandes Rosa de; Gonzales, João Carlos; Masuda, Hatisaburo; Oliveira, Pedro L.; Masudaa, Aoi

doi:10.1016/s0165-2427(98)00194-9

Cited by 67 publications

(41 citation statements)

References 21 publications

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“…Of the 4 I. scapularis pepsin-like enzymes, 2 (ISCW003823 and ISCW00023880) are provisionally identified as Cathepsin D. In mammals, cathepsin D is a multifunctional enzyme that is involved in regulating numerous biological processes ranging from protein turnover, apoptosis, cell signaling regulation, cancer pathogenesis (Vashishta et al, 2009; Benes et al, 2008). In ticks, cathepsin-D like enzymes have been linked to regulating important tick physiological functions: blood meal processing (Horn et al, 2009; Sojka et al, 2008; Boldbaatar et al, 2006) and reproduction through processing of vittelogenin and embryogenesis (Abreu et al, 2004; da Silva Vaz et al, 1998). The 10 I. scapularis aspartic proteases enzymes in clan AD are also from a single family, A22 (table 1), which is typified by presenilin-1 and the intramembrane protease aspartic protein (IMPAS)-1.…”

Section: Aspartic Proteasesmentioning

confidence: 99%

A snapshot of the Ixodes scapularis degradome

Mulenga

Erikson

2011

Gene

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Parasitic encoded proteases are essential to regulating interactions between parasites and their hosts and thus they represent attractive anti-parasitic druggable and/or vaccine target. We have utilized annotations of Ixodes scapularis proteases in gene bank and version 9.3 MEROPS database to compile an index of at least 233 putatively active and 150 putatively inactive protease enzymes that are encoded by the Ixodes scapularis genome. The 233 putatively active protease homologs hereafter referred to as the degradome (the full repertoire of proteases encoded by the I. scapularis genome) represents ~1.14% of the 20485 putative I. scapularis protein content. Consistent with observations in other animals, the content of the I. scapularis degradome is ~6.0% (14/233) aspartic, ~19% (44/233) cysteine, ~40% (93/233) Metallo, ~28.3% (66/233) serine and ~6.4% (15/233) threonine proteases. When scanned against other tick sequences, ~11% (25/233) of I. scapularis putatively active proteases are conserved in other tick species with ≥60% amino acid identity levels. The I. scapularis genome does not apparently encode for putatively inactive aspartic proteases. Of the 150 putative inactive protease homologs none are from the aspartic protease class, ~8% (12/150) are cysteine, ~58.7% (88/150) metallo, 30% (45/150) serine and ~3.3% (5/150) are threonine proteases. The I. scapularis tick genome appears to have evolutionarily lost proteolytic activity of at least 6 protease families, C56 and C64 (cysteine), M20 and M23 (metallo), S24 and S28 (serine) as revealed by a lack of the putatively active proteases in these families. The overall protease content is comparable to other organisms. However, the paucity of the S1 chymotrypsin/trypsin-like serine protease family in the I. scapularis genome where it is ~12.7% (28/233) of the degradome as opposed to ~22–48% content in other blood feeding arthropods, Pediculus humanus humanus, Anopheles gambiae, Aedes Aegypti and Culex pipiens quinquenfasciatus is notable. The data is presented as a one-stop index of proteases encoded by the I. scapularis genome.

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Section: Aspartic Proteasesmentioning

confidence: 99%

A snapshot of the Ixodes scapularis degradome

Mulenga

Erikson

2011

Gene

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“…Very briefly, an aspartic proteinase precursor from B. microplus eggs can confer partial protection (Da Silva Vaz et al 1998). In experiments with expression library immunization using cDNA from I. scapularis, one of the two unique cDNAs with putative function which gave some protection was an endopeptidase (Almazán et al.…”

Section: P R O T E I N a S E S A S V A C C I N E A N T I G E N Smentioning

confidence: 99%

Vaccination against ectoparasites

Willadsen

2006

Parasitology

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Ectoparasites of livestock are of great economic and social importance but their effective control remains difficult. The feasibility of vaccination as a novel control measure was established over a decade ago with the commercial release of a recombinant vaccine against the cattle tick Boophilus microplus. Since then, research has continued on ticks and other ectoparasites. While some ectoparasite species will undoubtedly be refractory to immunological control, for others there has been a steady accumulation of knowledge of partially protective antigens, now accelerating through the application of genomic technologies. Nevertheless, progress towards usable, commercially available vaccines has been limited by a number of factors. The number of highly effective antigens is still very small. Although some classes of antigen have been investigated in more detail than others, we have no systematic knowledge of what distinguishes an effective antigen. Much hope has been placed on the potential of multi-antigen mixtures to deliver the efficacy required of a successful vaccine but with little experimental evidence. The application of current knowledge across parasite and host species needs to be explored but little has been done. In most cases, the path to commercial delivery is uncertain. Although many constraints and challenges remain, the need for vaccines and our capacity to develop them can only increase.

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“…Several proteins, like Bm86 [13], Bm91 [14], Bm95 [15], BYC [16,17], GST [18] and VTDCE [19], have been tested as vaccine candidates to restrain R. microplus development. These proteins induce immune responses after cattle immunization, interfering with protein functions and decreasing tick viability, which makes them potential vaccine candidates [20].…”

Section: Introductionmentioning

confidence: 99%

Inhibition of Enzyme Activity of Rhipicephalus (Boophilus) microplus Triosephosphate Isomerase and BME26 Cell Growth by Monoclonal Antibodies

Saramago

Franceschi

Logullo

et al. 2012

IJMS

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In the present work, we produced two monoclonal antibodies (BrBm37 and BrBm38) and tested their action against the triosephosphate isomerase of Rhipicephalus (Boophilus) microplus (RmTIM). These antibodies recognize epitopes on both the native and recombinant forms of the protein. rRmTIM inhibition by BrBm37 was up to 85% whereas that of BrBrm38 was 98%, depending on the antibody-enzyme ratio. RmTIM activity was lower in ovarian, gut, and fat body tissue extracts treated with BrBm37 or BrBm38 mAbs. The proliferation of the embryonic tick cell line (BME26) was inhibited by BrBm37 and BrBm38 mAbs. In summary, the results reveal that it is possible to interfere with the RmTIM function using antibodies, even in intact cells.

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Immunization of bovines with an aspartic proteinase precursor isolated from Boophilus microplus eggs

Cited by 67 publications

References 21 publications

A snapshot of the Ixodes scapularis degradome

A snapshot of the Ixodes scapularis degradome

Vaccination against ectoparasites

Inhibition of Enzyme Activity of Rhipicephalus (Boophilus) microplus Triosephosphate Isomerase and BME26 Cell Growth by Monoclonal Antibodies

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