18 research outputs found
Notes on family-group names for bees (Hymenoptera: Apoidea)
No full textAbstract. Corrected authorships and dates are provided for four family-group names for bees based on previously unrecognized earlier usages that made them nomenclatorially available. Sagemehl is newly recognized as the author of family-group names based on Dasypoda Latreille (Melittidae: Dasypodainae), Macropis Panzer (Melittidae: Macropidinae), and Hylaeus Fabricius (Colletidae: Hylaeinae), and Kawall as the author the family-group name based on Melitta Kirby, thereby taking precedence over the subsequent use of similar names by Börner, Robertson, Vi-ereck, and Schenck, respectively. In addition, descriptions are provided for three new family-group taxa; Dieunomiini Engel, new tribe (Halictidae: Nomiinae), Eremaphantina Engel, new subtribe (Melittidae: Hesperapini), and Tarsaliini Engel, new tribe (Apidae: Apinae); and one new genus-group taxon, Eremaphantella Engel, new subgenus
Carolacton treatment causes delocalization of the cell division proteins PknB and DivIVa in Streptococcus mutans in vivo
No full textThe small inhibitory molecule Carolacton has been shown to cause chain formation and bulging in Streptococci, suggesting a defect in cell division, but it is not known how cell division is impaired on a molecular level. Fluorescent fusion proteins have successfully been applied to visualize protein localization and dynamics in vivo and have revolutionized our understanding of cell wall growth, cell division, chromosome replication and segregation. However, in Streptococci the required vectors are largely lacking. We constructed vectors for chromosomal integration and inducible expression of fluorescent fusion proteins based on GFP+ in S. mutans. Their applicability was verified using four proteins with known localization in the cell. We then determined the effect of Carolacton on the subcellular localization of GFP+ fusions of the cell division protein DivIVa and the serine-threonine protein kinase PknB. Carolacton caused a significant delocalization of these proteins from midcell, in accordance with a previous study demonstrating the Carolacton insensitive phenotype of a pknB deletion strain. Carolacton treated cells displayed an elongated phenotype, increased septum formation and a severe defect in daughter cell separation. GFP+ fusions of two hypothetical proteins (SMU_503 and SMU_609), that had previously been shown to be the most strongly upregulated genes after Carolacton treatment, were found to be localized at the septum in midcell, indicating their role in cell division. These findings highlight the importance of PknB as a key regulator of cell division in streptococci and indicate a profound impact of Carolacton on the coordination between peripheral and septal cell wall growth. The established vector system represents a novel tool to study essential steps of cellular metabolism
Evaluation of plant-produced Clostridium perfringens type D epsilon toxoid in a vaccine against enterotoxaemia in sheep
No full textEnterotoxaemia (pulpy kidney) is a common bacterial disease of sheep caused by Clostridium
perfringens type D epsilon toxin. It has mortality rates of up to 30% in non-vaccinated animals.
Current vaccines from whole cell cultures are expensive to manufacture and can induce local
inflammatory responses in sheep. They usually have reduced immunogenicity because of the
difficulty of standardising the inactivation step in vaccine manufacturing. In the current study,
we evaluated the safety and potency of a recombinant plant-made epsilon toxoid protein
(r-Etox) as an affordable and safer alternative vaccine for developing countries. Results of
injection site reactions, rectal temperature and toxin neutralisation test in single and prime–
boost inoculations of mice, guinea pigs and sheep suggest that the product is not toxic to
animals and could protect sheep against enterotoxaemia.Onderstepoort Biological Products
(OBP), the CSIR Parliamentary Grant and the Technology
Innovation Agency (TIA) of the Republic of South Africa.http://www.ojvr.orgam2017Plant Scienc
Evaluation of plant-produced <i>Clostridium perfringens</i> type D <i>epsilon</i> toxoid in a vaccine against enterotoxaemia in sheep
No full textEnterotoxaemia (pulpy kidney) is a common bacterial disease of sheep caused by Clostridium perfringens type D epsilon toxin. It has mortality rates of up to 30% in non-vaccinated animals. Current vaccines from whole cell cultures are expensive to manufacture and can induce local inflammatory responses in sheep. They usually have reduced immunogenicity because of the difficulty of standardising the inactivation step in vaccine manufacturing. In the current study, we evaluated the safety and potency of a recombinant plant-made epsilon toxoid protein (r-Etox) as an affordable and safer alternative vaccine for developing countries. Results of injection site reactions, rectal temperature and toxin neutralisation test in single and prime– boost inoculations of mice, guinea pigs and sheep suggest that the product is not toxic to animals and could protect sheep against enterotoxaemia.</jats:p
Evaluation of plant-produced <i>Clostridium perfringens</i> type D <i>epsilon</i> toxoid in a vaccine against enterotoxaemia in sheep
No full textEnterotoxaemia (pulpy kidney) is a common bacterial disease of sheep caused by Clostridium perfringens type D epsilon toxin. It has mortality rates of up to 30% in non-vaccinated animals. Current vaccines from whole cell cultures are expensive to manufacture and can induce local inflammatory responses in sheep. They usually have reduced immunogenicity because of the difficulty of standardising the inactivation step in vaccine manufacturing. In the current study, we evaluated the safety and potency of a recombinant plant-made epsilon toxoid protein (r-Etox) as an affordable and safer alternative vaccine for developing countries. Results of injection site reactions, rectal temperature and toxin neutralisation test in single and prime– boost inoculations of mice, guinea pigs and sheep suggest that the product is not toxic to animals and could protect sheep against enterotoxaemia
Efficient In Vitro and In Vivo Activity of Glyco-Engineered Plant-Produced Rabies Monoclonal Antibodies E559 and 62-71-3.
No full textRabies is a neglected zoonotic disease that has no effective treatment after onset of illness. However the disease can be prevented effectively by prompt administration of post exposure prophylaxis which includes administration of passive immunizing antibodies (Rabies Immune Globulin, RIG). Currently, human RIG suffers from many restrictions including limited availability, batch-to batch inconsistencies and potential for contamination with blood-borne pathogens. Anti-rabies monoclonal antibodies (mAbs) have been identified as a promising alternative to RIG. Here, we applied a plant-based transient expression system to achieve rapid, high level production and efficacy of the two highly potent anti-rabies mAbs E559 and 62-71-3. Expression levels of up to 490 mg/kg of recombinant mAbs were obtained in Nicotiana benthamiana glycosylation mutants by using a viral based transient expression system. The plant-made E559 and 62-71-3, carrying human-type fucose-free N-glycans, assembled properly and were structurally sound as determined by mass spectrometry and calorimetric density measurements. Both mAbs efficiently neutralised diverse rabies virus variants in vitro. Importantly, E559 and 62-71-3 exhibited enhanced protection against rabies virus compared to human RIG in a hamster model post-exposure challenge trial. Collectively, our results provide the basis for the development of a multi-mAb based alternative to RIG
Efficient In Vitro and In Vivo Activity of Glyco-Engineered Plant-Produced Rabies Monoclonal Antibodies E559 and 62-71-3 - Fig 2
No full textDeconvoluted spectrum of intact, reduced E559 LC (A) and intact, reduced E559 HC (B).Theoretical molecular weights for LC and HC indicated. Detected N-linked glycoforms are shown. The N-glycan nomenclature used was from www.proglycan.com.</p
Graphic depiction of <i>in vitro</i> Rabies neutralisation activity of mAbs E559 and 62-71-3.
No full textGraphic depiction of in vitro Rabies neutralisation activity of mAbs E559 and 62-71-3.</p
MAb E559 and 62-71-3 expression levels obtained using various combinations of either PVX or TMV-based expression vectors with either the murine (m) or rice alpha amylase (r) signal peptide.
No full textMAb E559 and 62-71-3 expression levels obtained using various combinations of either PVX or TMV-based expression vectors with either the murine (m) or rice alpha amylase (r) signal peptide.</p
Fifty percent end-point neutralisation activity (reciprocal titre) of E559 and 62-71-3 in a modified Rapid Fluorescent Focus Inhibition Test (RFFIT).
No full textFifty percent end-point neutralisation activity (reciprocal titre) of E559 and 62-71-3 in a modified Rapid Fluorescent Focus Inhibition Test (RFFIT).</p
