Provided are novel human-derived anti-huntingtin (HTT) antibodies and biotechnological derivatives thereof, preferably capable of binding mutated and/or aggregated HTT species and or fragments thereof, as well as methods related thereto. The human-derived anti-HTT antibodies and biotechnological derivatives can be used in pharmaceutical and diagnostic compositions for HTT targeted immunotherapy of Huntington Disease and diagnosis thereof.

The present application in one aspect provide Fc-containing polypeptide conjugates comprising an Fc-containing polypeptide conjugated to a conjugate moiety, wherein the Fc-containing polypeptide comprises an N-glycosylated Fc region comprising an acceptor glutamine residue flanked by an N-glycosylation site and wherein the conjugate moiety is conjugated to the Fc-containing polypeptide via the acceptor glutamine residue. Also provided are methods of making such Fc-containing polypeptide conjugates by using a wildtype or engineered transglutaminases. Further provided are engineered transglutaminases specifically designed for carrying out such reactions.

Herein is reported an antibody that specifically binds to human CD 19, wherein the antibody comprises (a) HVR-H1 comprising the amino acid sequence of SEQ ID NO: 03, (b) HVR-H2 comprising the amino acid sequence of SEQ ID NO: 11, (c) HVR-H3 comprising the amino acid sequence of SEQ ID NO: 05, (d) HVR-L1 comprising the amino acid sequence of SEQ ID NO: 20 or 28, (e) HVR-L2 comprising the amino acid sequence of SEQ ID NO: 07, and (f) HVR-L3 comprising the amino acid sequence of SEQ ID NO: 08, as well as methods of using the same.

A polypeptide containing an antibody Fc region variant which has an amino acid sequence in which an amino acid alteration at position 238 according to EU numbering is combined with other specific amino acid alteration(s), was found to have decreased binding activities to all activating FcγRs, in particular FcγRIIa (R type), while maintaining its FcγRIIb-binding activity, when compared to a polypeptide containing a native IgG Fc region.

The present invention relates to a novel protein comprising novel genes that is extracted from Burkholderia gladioli strain NGJ1. A nucleotide sequence encoding the novel protein is represented by sequence SEQ ID No. 1 and amino acid sequence of the novel protein is represented by the sequence SEQ ID No. 2 is further provided. A nucleotide sequence and the amino acid sequence are obtained from genetically engineered Bg_9562 gene. The novel protein as well as encoding gene is adapted for broad spectrum anti-fungal and mycophagous activities.

The present invention relates to methods and compositions for modulating glycosylation profile, such as the galactosylation profile, of recombinant proteins expressed by mammalian host cells during the cell culture process by supplementing cell culture media with a peracetyl galactose.

The present invention relates to antibodies or fragments thereof that specifically bind FcγRIIB, particularly human FcγRIIB, with greater affinity than the antibodies or fragments thereof bind FcγRIIA, particularly human FcγRIIA. The present invention also provides the use of an anti-FcγRIIB antibody or an antigen-binding fragment thereof, as a single agent therapy for the treatment, prevention, management, or amelioration of a cancer, preferably a B-cell malignancy, particularly, B-cell chronic lymphocytic leukemia or non-Hodgkin's lymphoma, an autoimmune disorder, an inflammatory disorder, an IgE-mediated allergic disorder, or one or more symptoms thereof. The invention provides methods of enhancing the therapeutic effect of therapeutic antibodies by administering the antibodies of the invention to enhance the effector function of the therapeutic antibodies. The invention also provides methods of enhancing efficacy of a vaccine composition by administering the antibodies of the invention.

Provided herein are heteromultimer constructs with reduced or silenced effector function. In an embodiment is provided a heteromultimer construct comprising an IgG Fc construct having a first and a second Fc polypeptide, each Fc polypeptide comprising a modified lower hinge region wherein: the modified lower hinge region of said first Fc polypeptide comprises at least one amino acid modification, the modified lower hinge region of said second Fc polypeptide comprises at least one amino acid modification which is different from at least one amino acid modification of said first Fc polypeptide, and the IgG Fc construct displays reduced binding to all Fcγ receptors and to C1q protein as compared to a corresponding parent IgG Fc construct. Also provided are methods of producing such heteromultimer constructs, and methods of reducing ADCC for an antibody construct by reducing effector function.

The present invention provides a method of making an antibody by identifying a circulating antibody with activity from a subject comprising i) subjecting biological fluid selected from the group consisting of blood, plasma and serum and combinations thereof from the subject to one or more rounds of affinity chromatography to purify the circulating antibody; ii) optionally further subjecting the circulating antibody to isoelectric focusing to purify the circulating antibody based on charge; iii) testing the purified circulating antibody for activity; iv) digesting the purified circulating antibody from parts i) or ii) to create an antibody fragment; v) subjecting the antibody fragment to mass spectrometry to generate a mass assignment and a deduced amino acid sequence of the antibody fragment; vi) comparing the deduced amino acid sequence with an amino acid sequence of an antibody generated from the subject's B-cells to identify an antibody sequence that matches the deduced amino acid sequence; vii) generating an antibody comprising light chain and heavy chain CDR sequences of the B-cell antibody that matches the deducted amino acid sequence of party vi); and viii) testing the antibody of part vii) for activity.

A mixed mode chromatography method for separating correctly folded from incorrectly folded conformations of a given protein is provided. The method is highly effective in separating correctly folded etanercept from incorrectly folded etanercept and aggregates in commercially attractive yields capable of affording etanercept preparations having very high purity in terms of correctly folded etanercept versus incorrectly folded etanercept. The invention is further directed to protein preparations and formulations comprising correctly folded proteins obtained using the present methods, and methods of treatment using the high purity preparations obtained from the mixed mode method.