Merck + Co., Inc.

Merck Sharp + Dohme Corp.

James C Cook, Iii

Kathrin Ute Jansen

Joseph G Joyce

William L McClements

Annaliesa Sybil Anderson

Michael P Neeper

Chitrananda Abeygunawardana

Henry Z Markus

Paul M Keller

Tessie Brown McNeely

Kathryn J Hofmann

Robert S Lowe

Donna Lorraine Montgomery

Hugh A George

Leslie Cope

Charlotte C Ip

Keith Roper

Qiuwei Xu

Jessica Ching-Yee Ling

Ernest Dale Lehman

Loren S Schultz

Karen M Grimm

Mark Rosolowsky

Craig T Przysiecki

Robert W Hepler

The present invention features polypeptides comprising an amino acid sequence structurally related to SEQ ID NO: 1 and uses of such polypeptides. SEQ ID NO: 1 is a truncated derivative of a full-lengthpolypeptide. The full-length naturally occurring polypeptide is referred to herein as full-length ORF1319e. A His-tagged derivative of SEQ ID NO: 1 was found to produce a protective immune response against

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A high molecular weight polysaccharide intracellular adhesin (SAE) antigen having the general structure of poly-1,6,&#x3b2;-2-amidoglucopyranoside, which is variable substituted with N-acetyl and O-succinyl substituents is described. Also, a method is given for isolating this antigen from. The SAE can be used in a vaccine, either alone, conjugated to an immunogenic protein, and/or with an immunogenic adjuvant.

Human Papillomavirus virus like particles (VLPs) have been constructed so that they contain a modified L2 protein. The L2 protein has been minimized and is fused to a second protein or peptide. The fused protein is incorporated into the VLP and the VLP can deliver the protein to a cell. The modified VLPs can be used to increase the breadth of immune response in vaccine preparations or to deliver other proteins of interest.

Protein delivery system using human papillomavirus virus-like particles

A process for purifying papillomavirus virus-like particles (VLPs) includes the step of passing a partially purified VLP-containing solution through a hydroxyapatite chromatography column. The VLPs are then eluted using a buffer containing phosphate anion. The advantages of this method include the recovery of a high yield of intact VLPs.

Process for purifying human papillomavirus virus-like particles

Recombinant expression vectors encoding the L1 and L2 proteins of papillomavirus, methods of making and using the recombinant proteins and purified virus-like particles comprised of the recombinant proteins are provided.

Recombinant papillomavirus vaccines

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Lansdale, PA, United States of America

James C Cook, Iii