The invention is in the field of delivery of transgenes to target cells using viral vectors, particularly in the field of gene therapy. Compositions have been identified which allow for oral administration of viral particles, particularly adenoviral particles.

A new, reliable, easily scalable and reproducible method for the production of recombinant butyrylcholinesterase (rBuChE) is provided. Through the utilization of a plant transfection procedure, various plant strains have been shown to generate effective and scalable amounts of rBuChE under acceptable manufacturing processes to permit reliable levels of such enzymes for desired nerve agent protection requirements (including tetrameric products). As well, such methods in engineered plant lines have shown suitable production of these enzymes in tetramer form with glycan formation and sialylation (for terminal groups) to allow for optimal potency against organophosphorus agent exposure as well as proper immunogenic response within the plant sources. The overall production method, including the transfection and production within mammalian cells, as well as the process steps involved for such a reliable sourcing platform from plants is thus encompassed within the invention.

A new, reliable, easily scalable and reproducible method for the production of recombinant butyrylcholinesterase (rBuChE) is provided. Through the utilization of a plant transfection procedure, various plant strains have been shown to generate effective and scalable amounts of rBuChE under acceptable manufacturing processes to permit reliable levels of such enzymes for desired nerve agent protection requirements (including tetrameric products). As well, such methods in engineered plant lines have shown suitable production of these enzymes in tetramer form with glycan formation and sialyalation (for terminal groups) to allow for optimal potency against organophosphorus agent exposure as well as proper immunogenic response within the plant sources. The overall production method, including the transfection and production within mammalian cells, as well as the process steps involved for such a reliable sourcing platform from plants is thus encompassed within the invention.

Provided herein are methods and recombinant expression systems for the production of recombinant glycoproteins that have increased sialic acid content and contain predominantly alpha2-6 sialic acid linkages. Also provided herein are recombinant glycoproteins that have an increased in vivo circulatory half-life. One potential application of the glycoproteins described herein is for the treatment and prophylaxis of poisoning by neurotoxins.

The present invention provides fungal proteases and improved fungal strains that are deficient in protease production.

Method and plants expressing increased levels of Butyrylcholinesterase (BChE) is described. The nucleic acid molecule encoding BChE is operably linked to a promoter preferentially expressing to the endosperm cells of the plant, another embodiment expression is targeted to the endoplasmic reticulum of plant cell(s), to the cell wall of the plant cell(s) or both.

Disclosed herein are methods for the large-scale production of a highly thermally stable acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). Additionally, the expression methods disclosed herein can produce ChE preparations consisting of extract or purified forms that can be produced in high amounts and are highly thermally stable. These ChE products can be used in vitro detection, detoxification and decontamination methods.

This document provides butyrylcholinesterases having an enhanced ability to hydrolyze acyl ghrelin as well as nucleic acids encoding such butyrylcholinesterases. This document also provides methods and materials for treating obesity and/or aggression. For example, methods for administering a nucleic acid encoding a wild-type or mutant butyrylcholinesterase having the ability to hydrolyze acyl ghrelin to a mammal under conditions wherein the level of acyl ghrelin within the mammal is reduced, under conditions wherein the rate of body weight gain of the mammal is reduced, under conditions wherein the mammal's level of aggression is reduced, and/or under conditions wherein the mammal's rate of developing stress-induced tissue damage are provided.

The present disclosure is directed to methods and systems for identifying different parts of enzyme structure that can be engineered and/or assisted by engineered technologies to improve the speed and efficiency of the catalyzed chemical reactions. More specifically, the present disclosure is directed to identifying and modifying distal surface regions that affect catalytic activity. These surface regions are identified and ranked for the impact on enzyme activity, based on the transfer of energy from the surface regions to the active site. Methods are described for improving the catalytic efficiency by improving the energy transfer to overcome the activation energy barrier. The methods described are also applicable for improving the stability of enzymes and development of appropriate enzyme immobilization protocols.

Provided are compositions, kits, and methods for delivering a proteinaceous cargo, or a protein or a peptide, or a drug or a marker, to or into a cell or to an individual in need thereof. In alternative embodiments, products of manufacture as provided herein comprise: (a) a recombinant bacterial Contractile Injection System (CIS) or a Metamorphosis Associated Contractile structure (MAC) formed or configured to comprise a tube having an inner core, (b) a Metamorphosis-Inducing Factor 1 (Mif1) protein positioned in the inner core of the tube of the CIS or MAC, (c) a chaperone 605 protein non-covalently associated with the Mif1 protein positioned in the inner core of the tube of the CIS or MAC, and (d) a proteinaceous cargo, or a heterologous protein or peptide, or compound, non-covalently associated or covalently associated or linked to the Mif1.