Bryce Chackerian, Ph.D.
Professor, UNM HSC, Leader Project #2
Mail: BRF 323
Phone: (505) 272-0269
Fax: (505) 272-6029
Bryce is a Professor in the University of New Mexico's Department of Molecular Genetics and Microbiology. As a post-doctoral fellow in Dr. John Schiller's laboratory at the National Cancer Institute he began his work on using Virus-like particles (VLPs) as platform for antigen display. His laboratory has shown that VLP presentation can enhance the immunogenicity of numerous target epitopes, including epitopes derived from self-antigens, which are normally subject to the mechanisms of B cell tolerance. His work has focused on the development of new vaccines against infectious agents, as well as self-antigens involved in chronic diseases.
The immune system is remarkably adept at mounting strong responses against invading microorganisms such as viruses and bacteria. At the same time, it has developed mechanisms to avoid reacting against the body's own components. One the ways that the immune system is able to distinguish between foreign invaders and self-proteins is by being able to recognize and respond to the structure of pathogens. Virus particles, for example, typically consist of one or more proteins organized into a highly repetitive, particulate structure. These sorts of structures are highly stimulatory to the immune system, resulting in the induction of strong antibody and T-cell responses.
Many viral structural proteins have the intrinsic ability to self-assemble into virus-like particles (VLPs) that closely resemble authentic virions. These VLPs mimic the structures of the viruses from which they were derived, but, because they lack a viral genome, are not infectious. VLPs make excellent vaccines for several reasons. First, they are antigenically similar to the viruses from which they were derived, meaning that they can often induce antibodies that are capable of blocking viral infection. Second, because they aren't infectious, they have excellent safety profiles. Third, their multivalent structure is capable of inducing very strong antibody responses. Two VLP-based vaccines, for Hepatitis B virus and Human Papillomavirus, are currently approved clinically, and many more VLP-based vaccines are in clinical development.
VLPs can also be used as platforms to increase the immunogenicity of practically any antigen. Display of an antigen at high density on the surface of a VLP can dramatically enhance the immunogenicity of that antigen. This technique can be used to target antigens from pathogens and it can even be used to target self-antigens, which are normally not immunogenic. This finding has made it possible to develop new vaccines with the goal of deliberately inducing immune responses against self-molecules that are involved in chronic diseases, including cancer, Alzheimer's disease, and rheumatoid arthritis, among others. The Chackerian lab, in collaboration with Dr. David Peabody's laboratory at UNM, has exploited VLPs derived from a family of viruses that infect bacteria. These bacteriophages are safe, they cannot infect humans, they can be produced at high yields, and they are amenable to the techniques of protein engineering that make them a highly useful vaccine platform. The Peabody and Chackerian laboratories have developed techniques that allow them to link diverse antigens to bacteriophage VLPs, making it relatively easy to apply the VLP technology to promising targets and develop new vaccines. As part of the EPIC-STI, we are continuing to develop a candidate next-generation human papillomavirus (HPV) vaccine that is broadly protective against diverse HPV types. In collaboration with other projects in the Center, we are using our platform technology to identify vaccines for Chlamydia trachomatis.
- Engineering virus-like particles as vaccine platforms.
Frietze KM, Peabody DS, Chackerian B.
Curr Opin Virol. 2016 Jun;18:44-9. doi: 10.1016/j.coviro.2016.03.001. Review. PMID: 27039982
- Optimized Formulation of a Thermostable Spray-Dried Virus-Like Particle Vaccine against Human Papillomavirus.
Saboo S, Tumban E, Peabody J, Wafula D, Peabody DS, Chackerian B, Muttil P.
Mol Pharm. 2016 May 2;13(5):1646-55. doi: 10.1021/acs.molpharmaceut.6b00072. PMID: 27019231
- Moving towards a new class of vaccines for non-infectious chronic diseases.
Chackerian B, Frietze KM.
Expert Rev Vaccines. 2016 May;15(5):561-3. doi: 10.1586/14760584.2016.1159136. No abstract available. PMID: 26919571
- Progress and prospects for L2-based human papillomavirus vaccines.
Jiang RT, Schellenbacher C, Chackerian B, Roden RB.
Expert Rev Vaccines. 2016 Jul;15(7):853-62. doi: 10.1586/14760584.2016.1157479. PMID: 26901354
- Identification of Anti-CA125 Antibody Responses in Ovarian Cancer Patients by a Novel Deep Sequence-Coupled Biopanning Platform.
Frietze KM, Roden RB, Lee JH, Shi Y, Peabody DS, Chackerian B.
Cancer Immunol Res. 2016 Feb;4(2):157-64. doi: 10.1158/2326-6066.CIR-15-0165. PMID: 26589767
- A cholesterol-lowering VLP vaccine that targets PCSK9.
Crossey E, Amar MJ, Sampson M, Peabody J, Schiller JT, Chackerian B, Remaley AT.
Vaccine. 2015 Oct 26;33(43):5747-55. doi: 10.1016/j.vaccine.2015.09.044. PMID: 26413878
- Identification of an Immunogenic Mimic of a Conserved Epitope on the Plasmodium falciparum Blood Stage Antigen AMA1 Using Virus-Like Particle (VLP) Peptide Display.
Crossey E, Frietze K, Narum DL, Peabody DS, Chackerian B.
PLoS One. 2015 Jul 6;10(7):e0132560. doi: 10.1371/journal.pone.0132560. PMID: 26147502
- Preclinical refinements of a broadly protective VLP-based HPV vaccine targeting the minor capsid protein, L2.
Tumban E, Muttil P, Escobar CA, Peabody J, Wafula D, Peabody DS, Chackerian B.
Vaccine. 2015 Jun 26;33(29):3346-53. doi: 10.1016/j.vaccine.2015.05.016. PMID: 26003490
- Affinity selection of epitope-based vaccines using a bacteriophage virus-like particle platform.
O'Rourke JP, Peabody DS, Chackerian B.
Curr Opin Virol. 2015 Apr;11:76-82. doi: 10.1016/j.coviro.2015.03.005. Review. PMID: 25829254
- Development of a mimotope vaccine targeting the Staphylococcus aureus quorum sensing pathway.
O'Rourke JP, Daly SM, Triplett KD, Peabody D, Chackerian B, Hall PR.
PLoS One. 2014 Nov 7;9(11):e111198. doi: 10.1371/journal.pone.0111198. Erratum in: PLoS One. 2015;10(2):e0118160. PMID: 25379726
- A malaria vaccine candidate based on an epitope of the Plasmodium falciparum RH5 protein.
Ord RL, Caldeira JC, Rodriguez M, Noe A, Chackerian B, Peabody DS, Gutierrez G, Lobo CA.
Malar J. 2014 Aug 18;13:326. doi: 10.1186/1475-2875-13-326. PMID: 25135070
- Why HIV virions have low numbers of envelope spikes: implications for vaccine development.
Schiller J, Chackerian B.
PLoS Pathog. 2014 Aug 7;10(8):e1004254. doi: 10.1371/journal.ppat.1004254. Review. No abstract available. PMID: 25101974
- Immunization with a consensus epitope from human papillomavirus L2 induces antibodies that are broadly neutralizing.
Tyler M, Tumban E, Dziduszko A, Ozbun MA, Peabody DS, Chackerian B.
Vaccine. 2014 Jul 23;32(34):4267-74. doi: 10.1016/j.vaccine.2014.06.054. PMID: 24962748
- The use of hybrid virus-like particles to enhance the immunogenicity of a broadly protective HPV vaccine.
Tyler M, Tumban E, Peabody DS, Chackerian B.
Biotechnol Bioeng. 2014 Dec;111(12):2398-406. doi: 10.1002/bit.25311. PMID: 24917327
- Second-generation prophylactic HPV vaccines: successes and challenges.
Tyler M, Tumban E, Chackerian B.
Expert Rev Vaccines. 2014 Feb;13(2):247-55. doi: 10.1586/14760584.2014.865523. Review. PMID: 24350614
- A universal virus-like particle-based vaccine for human papillomavirus: longevity of protection and role of endogenous and exogenous adjuvants.
Tumban E, Peabody J, Peabody DS, Chackerian B.
Vaccine. 2013 Sep 23;31(41):4647-54. doi: 10.1016/j.vaccine.2013.07.052. PMID: 23933337
- VLPs displaying a single L2 epitope induce broadly cross-neutralizing antibodies against human papillomavirus.
Tumban E, Peabody J, Tyler M, Peabody DS, Chackerian B.
PLoS One. 2012;7(11):e49751. doi: 10.1371/journal.pone.0049751. PMID: 23185426
- Genital delivery of virus-like particle and pseudovirus-based vaccines.
Cuburu N, Chackerian B.
Expert Rev Vaccines. 2011 Sep;10(9):1245-8. doi: 10.1586/erv.11.104. No abstract available. PMID: 21919611
- A pan-HPV vaccine based on bacteriophage PP7 VLPs displaying broadly cross-neutralizing epitopes from the HPV minor capsid protein, L2.
Tumban E, Peabody J, Peabody DS, Chackerian B.
PLoS One. 2011;6(8):e23310. doi: 10.1371/journal.pone.0023310. PMID: 21858066
- Aerosol delivery of virus-like particles to the genital tract induces local and systemic antibody responses.
Hunter Z, Tumban E, Dziduszko A, Chackerian B.
Vaccine. 2011 Jun 20;29(28):4584-92. doi: 10.1016/j.vaccine.2011.04.051. PMID: 21549786