Provided herein are multivalent particles and compositions of multivalent particles for blocking viral infection.

A fusion protein, comprising a variant angiotensin converting enzyme 2 (ACE2) domain covalently fused to a Fc domain. The variant ACE2 domain has a N-terminal deletion, a C-terminal deletion, or both, relative to a full-length wildtype ACE2 having a SEQ ID NO: 1. The variant ACE2 domain has ACE2 activity.

Provided herein are methods and compositions for treating a subject suffering from an enzyme deficiency in the central nervous system (CNS). The bifunctional fusion antibody provided herein comprise an antibody to an endogenous blood brain barrier (BBB) receptor and an enzyme deficient in mucopolysaccharidosis IIIB (MPS-IIIB). The fusion antibodies provided herein comprise alpha-N-acetylgulcosaminidase (NAGLU). The methods of treating an enzyme deficiency in the CNS comprise systemic administration of a fusion antibody provided herein.

The present disclosure provides ACE2-Fc fusion proteins comprising an ACE2 extracellular domain or fragment thereof and one or more Fc domains and methods of use thereof.

The present disclosure provides ACE2-Fc fusion proteins comprising an ACE2 extracellular domain or fragment thereof and one or more Fc domains and methods of use thereof.

The present invention relates to a lactic acid bacterium, in particular a strain of the Streptococcus genus, with reduced sensitivity to cos-type bacteriophages. The invention also relates to methods to engineer these lactic acid bacteria as well as their use to ferment milk.

The invention is directed to methods and compositions for the expression and purification of products such as peptides and proteins in microorganisms. In particular, pre-products are expressed recombinantly, wherein the cytoplasm of the microorganism alters the expressed pre-products to produce products in an active/final or otherwise desirable form. Alterations associated with expression of a desired recombinant product include shifting of the redox state of the cytoplasm to allow proper protein folding, site-directed cleavage of pre-proteins to activate the protein, site-directed cleavage of an unwanted methionine from the N terminus of the protein, and/or one or more ligations to form desired protein configurations, all within the same cell.

This invention is intended to improve glutathione productivity by fermentation using microorganisms. This invention relates to a microbial strain capable of overexpression of γ-glutamylcysteine, bis-γ-glutamylcystine, γ-glutamylcystine, reduced glutathione, and/or oxidized glutathione in which the expression level of a gene encoding serine-O-acetyltransferase (EC:2.3.1.30) is enhanced and a method involving the use of such microbial strain.

Compositions and methods for treating cancer are provided. In accordance with the instant invention, methods of inhibiting or treating cancer, particularly a “cold” cancer or a cancer lacking CD8+ tumor infiltrating lymphocytes (TILs) and/or other immunostimulatory features, in a subject are provided. In a particular embodiment, the method comprises administering an agent which increases ubiquitin-specific protease 6 (USP6) activity and/or expression to the subject.

This invention provides a tetrahedral antibody comprising a first, second, third, and fourth domain, wherein: a) each of the first and second domains are selected from the group consisting of a Fab domain and an Fc domain, b) each of the first and second domains comprise: i) a first polypeptide chain comprising a first N-terminus of the domain, and ii) a second polypeptide chain comprising a second N-terminus of the domain, c) the first N-terminus of the first domain and the first N-terminus of the second domain are joined to each other by a non-peptidyl linkage wherein the non-peptidyl linkage is: i) a covalent linkage, or ii) a non-covalent linkage between (1) a first dimerizing polypeptide attached by a peptide bond or via a peptide linker to the first N-terminus of the first domain, and (2) a second dimerizing polypeptide attached by a peptide bond or via a peptide linker to the first N-terminus of the second domain, wherein the first and second dimerizing polypeptides are not immunoglobulin polypeptides, d) the third domain is attached at its C-terminus by a peptide bond or via a peptide linker to: i) the second N-terminus of the first domain, or ii) the N-terminus of the first dimerizing polypeptide, and e) the fourth domain is attached at its C-terminus by a peptide bond or via a peptide linker to: i) the second N-terminus of the second domain, or ii) the N-terminus of the second dimerizing polypeptide.