The present invention relates to relates to T cell epitope peptides, proteins, nucleic acids and cells for use in immunother-apeutic methods. In particular, the present invention relates to the immunotherapy of viral infection. The present invention specifically relates to virus-associated T-cell peptide epitopes, alone or in combination with other virus-associated peptides that can serve as active pharmaceutical ingredients of vaccine compositions that stimulate anti-viral immune responses, or to stimulate T cells ex vivo and transfer into patients. Peptides bound to molecules of the major histocompatibility complex (MHC), or peptides as such, can also be targets of antibodies, soluble T-cell receptors, and other binding molecules.

The present disclosure relates to a method of modulating one or more genetically modified cells, e.g., chimeric antigen receptor (CAR)-expressing cells, ex vivo and/or in vivo.

The present invention provides methods for inducing regression of tumors in human subjects, the methods utilize a modified mesogenic strain of Newcastle disease virus (NDV) with modified F protein cleavage site, which is non-pathogenic to poultry (lentogenic), but exhibits oncolytic properties. The disclosed methods provide safe, effective and reliable means to induce regression of a tumor in an individual in need thereof. These methods overcome the drawbacks of using pathogenic strains of viruses for human therapy.

The invention provides a bidirectional hCMV-CAG4 promoter and recombinant vectors and recombinant virus comprising the bidirectional hCMV-CAG4 promoter operably linked to a first transgene in one direction and to a second transgene in the opposite direction. The invention also provides methods of making and using such recombinant vectors and recombinant virus.

HCMV US11 based therapeutics that can be used to target and reduce the activity of the FcRn protein are provided. Methods of treating auto-immune mediated and albumin-mediated diseases in a subject are provided that comprise administration of HCMV US11 protein, polypeptide fragments, or variants thereof, as well as methods for preventing, or treating, infections of HCMV through administration of a US11 inhibitor. US11 protein containing vaccine compositions are also provided for stimulation of an anti-US11 immune response for protection against HCMV infection.

The present invention relates to polypeptides and cytomegalovirus (CMV) antigens that include at least one introduced amino acid mutation relative to the amino acid sequence of the wild-type HCMV glycoprotein B (gB). In some embodiments, the polypeptide is stabilized in a conformation alternative to the gB postfusion conformation. Also disclosed are compositions including the polypeptides and uses thereof.

The disclosure describes HCMV ribonucleic acid (RNA) vaccines, as well as methods of using the vaccines and compositions comprising the vaccines.

This document provides methods and materials relating to isolated polypeptides, polypeptide preparations, vaccine preparations (e.g., anti-cancer vaccine preparations), and methods for vaccinating mammals. For example, polypeptides (e.g., CMV, MUC1, HER2, Mesothelin (MESO), TRAG-3, or CALR polypeptides) having the ability to be processed into different polypeptides such that the processed polypeptides as a group are capable of being presented by different MHC molecules present in a particular mammalian population are provided.

An expression system for expressing a herpesvirus glycoprotein complex including a vector inserted with two or more nucleic acid sequences that encode two or more subunits of a herpesvirus glycoprotein complex linked by one or more linking sequences such that the subunits are co-expressed simultaneously and self-processed to assemble into a glycoprotein complex. The expression system or the vector can be included in a vaccine composition. The vaccine composition can be used for preventing or treating herpesvirus infections.

This disclosure provides modified cytomegalovirus (CMV) gL proteins and complexes comprising gL proteins. The modified gL proteins remain intact and are able to form complexes with other CMV proteins.