Identification of heparin-binding amino acid residues in antibody HS4C3 with the potential to design antibodies against heparan sulfate domains.

Heparan sulfate (HS) is a linear polysaccharide with high structural and functional diversity. Detection and localization of HS in tissues can be performed using single chain variable fragment (scFv) antibodies. Although several anti-HS antibodies recognizing different sulfation motifs have been identified, little is known about their interaction with HS.

Development of prediction models for complications after primary total hip and knee arthroplasty: a single-centre retrospective cohort study in the Netherlands.

Objective: The aim of this study was to develop prediction models for patients with total hip arthroplasty (THA) and total knee arthroplasty (TKA) to predict the risk for surgical complications based on personal factors, comorbidities and medication use.

Design: Retrospective cohort study.

Setting: Tertiary care in outpatient clinic of university medical centre.

Construction and evaluation of an antibody phage display library targeting heparan sulfate.

Heparan sulfate (HS) is a linear polysaccharide with high structural diversity. Different HS epitopes have been detected and localized using single chain variable fragment (scFv) antibodies from a 'single pot' phage display library containing a randomized complementarity determining region of the heavy chain (CDR3). In this study, we created a new library containing anti-HS scFvs that all harbor a dp-38 heavy chain segment where the CDR3 region was engineered to contain the XBBXBX heparin binding consensus site (X = any amino acid, B = R, K or H).