Photo of Avelino Teixeira

Avelino Teixeira

  • ASSISTANT PROFESSOR Medicine, Cardiology
Print ProfilePrint Profile


  • NIH

  • Ph.D., University of Cape Town



The aim of my research is the development of technologies for the purification and identification of biologically important proteins that are difficult to isolate. To this end I develop and implement specific chromatographic strategies and assays to purify proteins and follow their progress through the purification steps. Pure proteins are then identified using mass spectrometric sequencing methods designed and optimized in my lab. To verify the identity of the protein(s) their genes are cloned and expressed and the purified recombinant protein tested in the assay(s) utilized in the initial purification. My research has contributed to two ongoing projects in the Department of Medicine.

1. Isolation and identification of proteins secreted by human CD8+ cells that suppress replication of the Human Immunodeficiency Virus (HIV-1)

The presence of suppressive factors secreted by human CD8+ cells been well documented. Although a number of proteins contributing to this suppression have been isolated and identified we and other groups have shown that the described factors do not fully account for the antiviral activity. In a collaborative effort, separation protocols have been designed and implemented to purify HIV-1 suppressive factors in biologically active form and identify them by mass spectrometry (LC/MS/MS). These methods have identified a very active suppressor protein as well as a number of potent suppressing chromatographic fractions which are currently being examined by mass spectrometry to determine their identities.

2. Isolation and identification of the components of a multi-component nucleic acid conducting channel present in the plasma membrane of a number of eukaryotic cell types

Membrane proteins, especially those whose function results from the concerted activity of a number of proteins are very challenging to purify particularly if biological activity is to be maintained for assay purposes. As part of a collaborative effort we have developed the necessary isolation protocols to isolate the entire channel complex in a biologically active form and have to date identified by mass spectrometry a number of the component proteins, one of which has been verified as part of the complex. Work continues currently to identify the transmembrane domain of this extremely important channel.

In addition, as an offshoot of my research work I run the Proteomics Laboratory of the Department of Medicine at Mount Sinai Medical Center which operates on a fee for service basis.

Overview of the Proteomics Laboratory:

  • The goal of the Proteomics Laboratory is to provide rapid, reliable and reasonably priced protein separation and identification services and technical support to researchers in the biomedical field.
  • While the Proteomics Laboratory is part of the Department of Medicineand its services are available primarily to the Mount Sinai Medical Center community projects from other institutions are welcomed.

For more information, please visit the Proteomics Laboratory website.


Hanss B, Leal-Pinto E, Teixeira A, Tran B, Lee CH, Henderson SC, Klotman PE. Localization of the nucleic acid channel regulatory subunit cytosolic malate dehydrogenase. J Memb. Biol 2008; 226: 1-8.

Mosoian A, Teixeira A, Burns CS, Khitrov G, Zhang W, Gusella L, Klotman P, Klotman M. Influence of prothymosin-alpha on HIV-1 target cells. Ann. N.Y. Acad. Sci 2007; 1112: 269-285.

Mosoian A, Teixeira A, High AA, Christian RE, Hunt DF, Shabanowitz J, Liu X, Klotman M. A novel function of prothymosin alpha as a potent Inhibitor of HIV-1 gene expression in primary macrophages. J Virol 2006; 80: 9200-9206.

Leal-Pinto E, Teixeira A, Tran B, Hanss B, Klotman PE. Presence of the nucleic acid channel in renal brush-border membranes: allosteric modulation by extracellular calcium. Am. J. Physiol 2005; 289: F97-F106.

Hanss B, Leal-Pinto E, Teixeira A, Christian RE, Shabanowitz J, Hunt DF, Klotman PE. Cytosolic malate dehydrogenase confers selectivity of the nucleic acid-conducting channel. Proc Natl Acad Sci U S A 2002; 99: 1707-1712.

Schwartz EJ, Neumann AU, Teixeira AV, Bruggeman LA, Rappaport J, Perelson AS, Klotman PE. Effect of target cell availability on HIV-1 production in vitro. AIDS 2002; 16: 341-345.

Mosoian A, Teixeira A, Caron E, Piwoz J, Klotman ME. CD8+ cell lines isolated from HIV-1-infected children have potent soluble HIV-1 inhibitory activity that differs from beta -chemokines. Viral Immunology 2000; 13: 481-495.

Industry Relationships

Physicians and scientists on the faculty of the Icahn School of Medicine at Mount Sinai often interact with pharmaceutical, device and biotechnology companies to improve patient care, develop new therapies and achieve scientific breakthroughs. In order to promote an ethical and transparent environment for conducting research, providing clinical care and teaching, Mount Sinai requires that salaried faculty inform the School of their relationships with such companies.

Dr. Teixeira did not report having any of the following types of financial relationships with industry during 2014 and/or 2015: consulting, scientific advisory board, industry-sponsored lectures, service on Board of Directors, participation on industry-sponsored committees, equity ownership valued at greater than 5% of a publicly traded company or any value in a privately held company. Please note that this information may differ from information posted on corporate sites due to timing or classification differences.

Mount Sinai's faculty policies relating to faculty collaboration with industry are posted on our website. Patients may wish to ask their physician about the activities they perform for companies.

Edit profile in Sinai Central


Annenberg Building Floor 18 Room 94
1468 Madison Avenue
New York, NY 10029

Tel: 212-241-3110