Max Crispin

This study shows that xenoglycosylation of HIV-1 Env with core (1,3)-fucose enhances cross-clade neutralization and diversifies human antibody lineages.

This paper develops a computational method to design glycoproteins with controlled N-linked glycan composition by encoding glycan location and structure into amino acid sequences.

This paper develops a consensus HCV E1E2 antigen that engages germline B cell precursors of broadly neutralizing antibodies.

The paper maps glycan composition across HIV-1 pseudoviruses to show how sequence diversity affects the glycan shield and its vulnerability to broadly neutralizing antibodies.

Epitope-focused S2 stem-helix nanoparticle immunogens elicit protective broadly neutralizing antibodies against diverse betacoronaviruses in non-human primates, establishing a framework for pan-betacoronavirus vaccines.

This paper describes the development and cGMP manufacturing of an HIV vaccine candidate for clinical trials, demonstrating scalable production and quality control.

This study shows that a germline-targeting HIV immunogen induces cross-neutralizing antibodies in outbred macaques by priming V2-apex bnAb B cell precursors.

This study uses cryoEM and machine learning to predict and redirect immunodominant epitopes in HIV Env, showing improved vaccine antigen design.

This study shows that STT3A is more critical than STT3B for HIV-1 Env glycosylation, affecting virus production and antibody sensitivity.

The paper designs, characterizes, and tests a soluble HCV E1E2 heterodimer and self-assembling nanoparticles for vaccine development.

This paper demonstrates the feasibility of expressing monoclonal IgG and IgA antibodies in non-human primates using mRNA-LNPs, showing both isotypes retain HIV-neutralizing function and native-like glycosylation.

The paper investigates how B cell affinity affects germinal center (GC) responses by showing high-affinity B cells have shorter GC residence times and lower-affinity B cells are maintained, suggesting an antibody feedback mechanism that modulates affinity and epitope spreading.

This paper designs self-assembling protein nanoparticle vaccines using AlphaFold2 predictions, demonstrating atomic-level accuracy and potent immune responses in mice.

The paper designs native-like HIV Env single-chain trimers (SCTs) that are stable, immunogenic, and compatible with vaccine delivery methods.

This study shows a novel two-step mechanism for inducing broadly neutralizing HIV antibodies in macaques using a modified SHIV, informing vaccine design.

This paper identifies sequence determinants that regulate oligosaccharyltransferase (OST) catalytic efficiency and glycosylation specificity in proteins.

This paper identifies Mann-type DLBCL as a subtype of GCB-DLBCL characterized by oligomannose-type glycans in CDR-located AGS, associated with poor prognosis and distinct gene expression patterns.

This study shows that targeting the conserved HIV fusion peptide with modified Env immunogens in rhesus macaques can focus immune responses on neutralizing epitopes.

This study shows that a single immunization with a germline-targeting trimer can induce broad HIV-1 neutralizing antibodies in a rhesus macaque bnAb mouse model.

This study rationally designs and characterizes filovirus glycoproteins and nanoparticles in vitro and in vivo to aid vaccine development.

This study stabilizes an HIV-1 clade C trimer using multiple platforms and shows improved antigenic and immunogenic properties.

This study evaluates glycoengineered HIV-1 trimers to enhance bNAb recognition, finding that B4GalT1+ST6GalT1 modifications increase antibody titers in infected donors but reduce vaccine-induced neutralizing antibodies.

The paper examines how natural variations in SARS-CoV-2 glycan sites affect spike protein dynamics and antigenic structure through molecular dynamics and structural modeling.

The paper identifies a novel short ACE2 isoform expressed in respiratory epithelia that is upregulated by interferon and RNA virus infection but not SARS-CoV-2, and shows reduced SARS-CoV-2 binding affinity.